ΠΠΎΠ²ΡΠΉ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ ΠΎΡΡΠΎ-ΠΏΡΡΡ Ρ Rhodococcus ΠΎpacus ICP, ΡΠ°ΡΡΡΡΠ΅Π³ΠΎ Π½Π° 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π΅: ΡΠ½Π·ΠΈΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΈ Π³Π΅Π½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ Π°ΡΠΏΠ΅ΠΊΡΡ
ΠΠ΅ΡΠΎΠ΄ΠΎΠΌ 19F-^MP ΠΏΠΎΠ΄ΡΠ²Π΅ΡΠΆΠ΄Π΅Π½Π° ΡΡΠ½ΠΊΡΠΈΡ ΠΊΠ°ΠΆΠ΄ΠΎΠ³ΠΎ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ° 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ R. opacus 1 Π‘Π . ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π° ΠΎΡΡΡΠ΅ΡΡΠ²Π»ΡΠ΅Ρ Π΄Π΅Π³Π°Π»ΠΎΠ³Π΅ΠΈΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ Π³Π°Π»ΠΎΠΌΡΠΊΠΎΠ½Π°ΡΠΎΠ² Ρ ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ Π³/Π½Π±-Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½Π°. ΠΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½Ρ ΠΈ ΡΠ΅ΠΊΠ²Π΅Π½ΠΈΡΠΎΠ²Π°Π½Ρ Π³Π΅Π½Ρ, ΠΊΠΎΠ΄ΠΈΡΡΡΡΠΈΠ΅ ΡΠ΅ΡΠΌΠ΅Π½ΡΡ 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΠΏΡ-ΠΏΡΡΠΈ R. opacus 1Π‘Π . ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ ΠΎΠ½ΠΈ… Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
- Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- ΠΡΠ΄Π΅ΡΠΆΠΊΠ°
- ΠΠΈΡΠ΅ΡΠ°ΡΡΡΠ°
- ΠΡΡΠ³ΠΈΠ΅ ΡΠ°Π±ΠΎΡΡ
- ΠΠΎΠΌΠΎΡΡ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈ
Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- Π‘ΠΏΠΈΡΠΎΠΊ ΡΠΎΠΊΡΠ°ΡΠ΅Π½ΠΈΠΉ
- ΠΠ±Π·ΠΎΡ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- ΠΠ»Π°Π²Π° 1. ΠΠ½Π·ΠΈΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΈ Π³Π΅Π½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ Π°ΡΠΏΠ΅ΠΊΡΡ ΠΏΡΠ΅Π²ΡΠ°ΡΠ΅Π½ΠΈΡ ΡΠ΅Π½ΠΎΠ»ΠΎΠ² ΠΈ Ρ
Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠ² Π±Π°ΠΊΡΠ΅ΡΠΈΡΠΌΠΈ. Π
- 1. 1. Π€Π΅Π½ΠΎΠ»Ρ ΠΈ Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Ρ — ΠΏΡΠΈΠΎΡΠΈΡΠ΅ΡΠ½ΡΠ΅ ΠΏΠΎΠ»Π»ΡΡΠ°Π½ΡΡ ΠΎΠΊΡΡΠΆΠ°ΡΡΠ΅ΠΉ ΡΡΠ΅Π΄Ρ
- 1. 2. ΠΠ°ΠΊΡΠ΅ΡΠΈΠΈ ΡΠΎΠ΄Π° Rhoclococcus — ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΡΠ΅ Π΄Π΅ΡΡΡΡΠΊΡΠΎΡΡ ΠΏΠΎΠ»Π»ΡΡΠ°Π½ΡΠΎΠ²
- 1. 3. ΠΡΠ½ΠΎΠ²Π½ΡΠ΅ ΠΏΡΡΠΈ ΠΏΡΠ΅Π²ΡΠ°ΡΠ΅Π½ΠΈΡ ΡΠ΅Π½ΠΎΠ»ΠΎΠ² ΠΈ Ρ
Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠ² ΠΌΠΈΠΊΡΠΎΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠ°ΠΌΠΈ
- 1. 3. 1. ΠΠ΅ΡΠ°-ΠΏΡΡΡ ΡΠ°ΡΡΠ΅ΠΏΠ»Π΅Π½ΠΈΡ ΠΊΠ°ΡΠ΅Ρ ΠΎΠ»Π°
- 1. 3. 2. ΠΠ»Π°ΡΡΠΈΡΠ΅ΡΠΊΠΈΠΉ ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ opwo-nym ΡΠ°ΡΡΠ΅ΠΏΠ»Π΅Π½ΠΈΡ ΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΠΎΠ²
- 1. 4. ΠΠ΅Π½Π΅ΡΠΈΠΊΠ° Π±ΠΈΠΎΠ΄Π΅Π³ΡΠ°Π΄Π°ΡΠΈΠ²Π½ΡΡ
ΠΏΡΡΠ΅ΠΉ ΠΊΠ°ΡΠ΅Ρ
ΠΎΠ»Π° ΠΈ Ρ
Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ
ΠΎΠ»ΠΎΠ²
- 1. 4. 1. Π‘ΡΡΡΠΊΡΡΡΠ° Π³Π΅Π½Π½ΡΡ ΠΊΠ»Π°ΡΡΠ΅ΡΠΎΠ² ΠΊΠ°ΡΠ°Π±ΠΎΠ»ΠΈΠ·ΠΌΠ° ΠΊΠ°ΡΠ΅Ρ ΠΎΠ»Π° ΠΈ 4-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»Π° Ρ Rhodococcus opacus 1Π‘Π
- 1. 4. 2. Π‘ΡΠ°Π²Π½Π΅Π½ΠΈΠ΅ Ρ Π±ΠΈΠΎΠ΄Π΅Π³ΡΠ°Π΄Π°ΡΠΈΠ²Π½ΡΠΌΠΈ ΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΡΠΌΠΈ ΠΈ Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΡΠΌΠΈ ΠΎΠΏΠ΅ΡΠΎΠ½Π°ΠΌΠΈ Π΄ΡΡΠ³ΠΈΡ ΠΏΡΠΎΡΠ΅ΠΎΠ±Π°ΠΊΡΠ΅ΡΠΈΠΉ
- 1. 4. 3. Π Π΅Π³ΡΠ»ΡΡΠΈΡ ΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠ³ΠΎ ΠΈ Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠ³ΠΎ ΠΎΠΏΠ΅ΡΠΎΠ½ΠΎΠ² Π±Π΅Π»ΠΊΠ°ΠΌΠΈ — Π°ΠΊΡΠΈΠ²Π°ΡΠΎΡΠ°ΠΌΠΈ
- 2. 1. Π Π΅Π°ΠΊΡΠΈΠ²Ρ
- 2. 2. Π¨ΡΠ°ΠΌΠΌΡ, ΠΈΡΠΏΠΎΠ»ΡΠ·ΠΎΠ²Π°Π½Π½ΡΠ΅ Π² ΡΠ°Π±ΠΎΡΠ΅
- 2. 3. ΠΡΠ»ΡΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΡΡΠ°ΠΌΠΌΠΎΠ²
- 2. 4. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ² ΠΈ ΠΌΠ΅ΡΠΎΠ΄Ρ ΠΈΡ
ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ
- 2. 4. 1. ΠΠ½Π°Π»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΌΠ΅ΡΠΎΠ΄Ρ
- 2. 4. 2. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ Π±Π΅ΡΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ ΡΠΊΡΡΡΠ°ΠΊΡΠΎΠ² ΠΈ ΠΎΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΊΠΎΠ½ΡΠ΅Π½ΡΡΠ°ΡΠΈΠΈ Π±Π΅Π»ΠΊΠ°
- 2. 4. 3. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ²
- 2. 4. 4. ΠΡΠΈΡΡΠΊΠ° ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ²
- 2. 4. 4. 1. ΠΡΠΈΡΡΠΊΠ° 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Ρ.5 !
- 2. 4. 4. 2. ΠΡΠΈΡΡΠΊΠ° 2-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ ΡΠΈΠΊΠ»ΠΎΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Ρ
- 2. 4. 4. 3. ΠΡΠΈΡΡΠΊΠ° 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Ρ
- 2. 4. 4. 4. ΠΡΠΈΡΡΠΊΠ° Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Ρ
- 2. 4. 4. 5. ΠΡΠΈΡΡΠΊΠ° ΡΠ΅Π½ΠΎΠ» Π³ΠΈΠ΄ΡΠΎΠΊΡΠΈΠ»Π°Π·Ρ
- 2. 4. 5. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΠΈΠ·ΠΈΠΊΠΎ-Ρ
ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΡ
ΡΠ²ΠΎΠΉΡΡΠ² ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ²
- 2. 4. 5. 1. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΡΠ±ΡΠ΅Π΄ΠΈΠ½ΠΈΡΠ½ΠΎΠ³ΠΎ ΠΈ ΠΌΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΠΎΠ³ΠΎ Π²Π΅ΡΠ° ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ²
- 2. 4. 5. 2. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΠ- ΠΈ ΡΠ΅ΠΌΠΏΠ΅ΡΠ°ΡΡΡΠ½ΡΡ ΠΎΠΏΡΠΈΠΌΡΠΌΠΎΠ² ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ²
- 2. 4. 5. 3. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΠΠΠ’Π Π½Π° Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Ρ
- 2. 4. 6. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΊΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΡ Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΡΡΠΈΠΊ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ²
- 2. 5. ΠΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΈ ΡΠ΅ΠΊΠ²Π΅Π½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ Π³Π΅Π½ΠΎΠ² 3-Ρ
Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ
ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ
- 2. 5. 1. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅, Π²ΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΈ ΡΠ΅ΠΊΠ²Π΅Π½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΏΠ΅ΠΏΡΠΈΠ΄ΠΎΠ² 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Ρ
- 2. 5. 2. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ Ρ ΡΠΎΠΌΠΎΡΠΎΠΌΠ½ΠΎΠΉ ΠΈ ΠΏΠ»Π°Π·ΠΌΠΈΠ΄Π½ΡΡ ΠΠΠ, ΠΏΡΠΈΠ³ΠΎΡΠΎΠ²Π»Π΅Π½ΠΈΠ΅ Π’-Π²Π΅ΠΊΡΠΎΡΠ° ΠΈ Π²ΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΡΠ°Π³ΠΌΠ΅Π½ΡΠΎΠ² ΠΠΠ
- 2. 5. 3. ΠΠΌΠΏΠ»ΠΈΡΠΈΠΊΠ°ΡΠΈΡ ΡΡΠ°Π³ΠΌΠ΅Π½ΡΠ° 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Π½ΠΎΠ³ΠΎ Π³Π΅Π½Π°
- 2. 5. 4. ΠΡΠΈΠ³ΠΎΡΠΎΠ²Π»Π΅Π½ΠΈΠ΅ ΠΊΠΎΠΌΠΏΠ΅ΡΠ΅Π½ΡΠ½ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ E. coli DH5a ΠΈ ΠΈΡ ΡΡΠ°Π½ΡΡΠΎΡΠΌΠ°ΡΠΈΡ
- 2. 5. 5. ΠΠ»ΠΎΡΠ³ΠΈΠ½Π³ΠΈ, Π³ΠΈΠ±ΡΠΈΠ΄ΠΈΠ·Π°ΡΠΈΠΈ ΠΈ ΠΊΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅
- 2. 5. 6. Π‘ΠΈΠΊΠ²Π΅Π½Ρ ΠΊΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΉ ΠΠΠ ΠΈ Π΅Π³ΠΎ Π°Π½Π°Π»ΠΈΠ·
- 3. 1. ΠΠ΄Π°ΠΏΡΠ°ΡΠΈΡ ΠΈ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ ΡΠΎΡΡΠ° R. opacus 1Π‘Π Π½Π° 2- ΠΈ 3-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π°Ρ ΠΈ 3-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠ΅
- 3. 2. ΠΡΡΠΈ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΡ 2- ΠΈ 3-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠ² ΠΈ 3-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠ° R. opacus 1Π‘Π
- 3. 3. Π€Π΅ΡΠΌΠ΅Π½ΡΡ 3-Ρ
Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ
ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ qpwo-ΠΏΡΡΠΈ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΡ 2-Ρ
Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π° It opacus 1Π‘Π
- 3. 3. 1. Π-Π₯Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ
ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Π°
- 3. 3. 1. 1. ΠΡΠΈΡΡΠΊΠ° ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°
- 3. 3. 1. 2. Π’Π΅ΠΌΠΏΠ΅ΡΠ°ΡΡΡΠ½ΡΠΉ ΠΈ ΡΠ-ΠΎΠΏΡΠΈΠΌΡΠΌΡ.,
- 3. 3. 1. 3. ΠΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΊΠΎΠ½ΡΡΠ°Π½ΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°
- 3. 3. 2. 2-Π₯Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ ΡΠΈΠΊΠ»ΠΎΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π°
- 3. 3. 2. 1. ΠΡΠΈΡΡΠΊΠ° ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°
- 3. 3. 2. 2. Π’Π΅ΠΌΠΏΠ΅ΡΠ°ΡΡΡΠ½ΡΠΉ ΠΈ ΡΠ-ΠΎΠΏΡΠΈΠΌΡΠΌΡ
- 3. 3. 2. 3. ΠΡΠ΅Π²ΡΠ°ΡΠ΅Π½ΠΈΠ΅ 2-Ρ Π»ΠΎΡ-1/ΠΈΡ,?/ΠΌΡ-ΠΌΡΠΊΠΎΠ½Π°ΡΠ° Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ ΡΠΈΠΊΠ»ΠΎΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·ΠΎΠΉ
- 3. 3. 2. 4. ΠΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΊΠΎΠ½ΡΡΠ°Π½ΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°
- 3. 3. 3. 5-Π₯Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π°
- 3. 3. 3. 1. ΠΡΠΈΡΡΠΊΠ° ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°
- 3. 3. 3. 2. ΠΡΠ΅Π²ΡΠ°ΡΠ΅Π½ΠΈΠ΅ 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½Π° 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·ΠΎΠΉ
- 3. 3. 4. ΠΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Π°
- 3. 3. 4. 1. ΠΡΠΈΡΡΠΊΠ° ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°
- 3. 3. 4. 2. Π’Π΅ΠΌΠΏΠ΅ΡΠ°ΡΡΡΠ½ΡΠΉ ΠΈ ΡΠ-ΠΎΠΏΡΠΈΠΌΡΠΌΡ
- 3. 3. 4. 3. ΠΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΊΠΎΠ½ΡΡΠ°Π½ΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°
- 3. 3. 4. 4. ΠΠ»ΠΈΡΠ½ΠΈΠ΅ ΠΠΠ’Π Π½Π° Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Ρ
- 3. 3. 1. Π-Π₯Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ
ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Π°
- 3. 4. 1. ΠΡΠΈΡΡΠΊΠ° ΡΠ΅Π½ΠΎΠ» Π³ΠΈΠ΄ΡΠΎΠΊΡΠΈΠ»Π°Π·Ρ ΠΈΠ· Trichosporon cutaneum
- 3. 4. 2. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ ΡΡΠΎΡΠ·Π°ΠΌΠ΅ΡΠ΅Π½Π½ΡΡ ΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΠΎΠ²
- 3. 4. 3. Π‘ΡΠ±ΡΡΡΠ°ΡΠ½Π°Ρ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ½ΠΎΡΡΡ 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Ρ
- 3. 4. 4. Π‘ΡΠ±ΡΡΡΠ°ΡΠ½Π°Ρ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ½ΠΎΡΡΡ 2-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ ΡΠΈΠΊΠ»ΠΎΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Ρ
- 3. 4. 5. ΠΡΠ΅Π²ΡΠ°ΡΠ΅Π½ΠΈΠ΅ 5-ΡΡΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½Π° 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·ΠΎΠΉ
- 3. 5. 1. ΠΠΎΠ½ΡΡΡΡΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΏΡΠ°ΠΉΠΌΠ΅ΡΠΎΠΈ Π΄Π»Ρ Π°ΠΌΠΏΠ»ΠΈΡΠΈΠΊΠ°ΡΠΈΠΈ ΡΡΠ°Π³ΠΌΠ΅Π½ΡΠ° Π³Π΅Π½Π° 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Ρ
- 3. 5. 2. ΠΠΌΠΏΠ»ΠΈΡΠΈΠΊΠ°ΡΠΈΡ ΠΈ ΡΠ΅ΠΊΠ²Π΅Π½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΡΡΠ°Π³ΠΌΠ΅Π½ΡΠ° Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Π½ΠΎΠ³ΠΎ Π³Π΅Π½Π°
- 3. 5. 3. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ ΠΊΠ»ΠΎΠ½Π°Π coli DH5a Ρ ΠΏΠ»Π°Π·ΠΌΠΈΠ΄ΠΎΠΉ, Π½Π΅ΡΡΡΠ΅ΠΉ ΡΡΠ°Π³ΠΌΠ΅Π½Ρ Ρ ΡΠΎΠΌΠΎΡΠΎΠΌΠ½ΠΎΠΉ ΠΠΠ Π opacus 1Π‘Π , ΠΊΠΎΠ΄ΠΈΡΡΡΡΠΈΠΉ ΡΡΠ°Π³ΠΌΠ΅Π½Ρ Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Π½ΠΎΠ³ΠΎ Π³Π΅Π½Π°
- 3. 5. 4. ΠΠ°ΡΡΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΈ ΠΎΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄Π½ΠΎΠΉ ΠΏΠΎΡΠ»Π΅Π΄ΠΎΠ²Π°ΡΠ΅Π»ΡΠ½ΠΎΡΡΠΈ Π²ΡΡΠ°Π²ΠΊΠΈ pROPl
ΠΠΎΠ²ΡΠΉ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ ΠΎΡΡΠΎ-ΠΏΡΡΡ Ρ Rhodococcus ΠΎpacus ICP, ΡΠ°ΡΡΡΡΠ΅Π³ΠΎ Π½Π° 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π΅: ΡΠ½Π·ΠΈΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΈ Π³Π΅Π½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ Π°ΡΠΏΠ΅ΠΊΡΡ (ΡΠ΅ΡΠ΅ΡΠ°Ρ, ΠΊΡΡΡΠΎΠ²Π°Ρ, Π΄ΠΈΠΏΠ»ΠΎΠΌ, ΠΊΠΎΠ½ΡΡΠΎΠ»ΡΠ½Π°Ρ)
ΠΠΊΡΡΠ°Π»ΡΠ½ΠΎΡΡΡ ΠΏΡΠΎΠ±Π»Π΅ΠΌΡ. Π’ΡΡΠ΄Π½ΠΎΡΠ°Π·Π»Π°Π³Π°Π΅ΠΌΡΠ΅ ΠΈ ΡΠΎΠΊΡΠΈΡΠ½ΡΠ΅ Ρ Π»ΠΎΡΠ°ΡΠΎΠΌΠ°Π³ΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΡ Π² Π±ΠΎΠ»ΡΡΠΈΡ ΠΊΠΎΠ»ΠΈΡΠ΅ΡΡΠ²Π°Ρ ΠΏΠΎΡΡΡΠΏΠ°ΡΡ Π² ΠΎΠΊΡΡΠΆΠ°ΡΡΡΡ ΡΡΠ΅Π΄Ρ Π² ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠ΅ Ρ ΠΎΠ·ΡΠΉΡΡΠ²Π΅Π½Π½ΠΎΠΉ Π΄Π΅ΡΡΠ΅Π»ΡΠ½ΠΎΡΡΠΈ ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°. ΠΠ΄Π½ΠΈΠΌΠΈ ΠΈΠ· ΡΠ°ΠΊΠΈΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ ΡΠ²Π»ΡΡΡΡΡ Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Ρ, ΡΠΈΡΠΎΠΊΠΎ ΠΈΡΠΏΠΎΠ»ΡΠ·ΡΠ΅ΠΌΡΠ΅ ΠΏΡΠΈ ΠΏΡΠΎΠΈΠ·Π²ΠΎΠ΄ΡΡΠ²Π΅ ΠΏΠ΅ΡΡΠΈΡΠΈΠ΄ΠΎΠ² ΠΈ Π΄Π»Ρ ΠΊΠΎΠ½ΡΠ΅ΡΠ²Π°ΡΠΈΠΈ Π΄ΡΠ΅Π²Π΅ΡΠΈΠ½Ρ. ΠΡΠΎΠ±Π»Π΅ΠΌΠ° ΡΡΠΈΠ»ΠΈΠ·Π°ΡΠΈΠΈ ΡΡΠΈΡ ΡΠΎΠΊΡΠΈΡΠ½ΡΡ ΠΊΡΠ΅Π½ΠΎΠ±ΠΈΠΎΡΠΈΠΊΠΎΠ² Π½Π° ΡΠ΅Π³ΠΎΠ΄Π½ΡΡΠ½ΠΈΠΉ Π΄Π΅Π½Ρ Π΄Π°Π»Π΅ΠΊΠ° ΠΎΡ ΠΏΠΎΠ»Π½ΠΎΠ³ΠΎ ΡΠ°Π·ΡΠ΅ΡΠ΅Π½ΠΈΡ. Π‘ΡΠ΅Π΄ΠΈ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠ², ΠΏΡΠΈΠΌΠ΅Π½ΡΠ΅ΠΌΡΡ Π΄Π»Ρ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΡ Ρ Π»ΠΎΡΠΈΡΠΎΠ²Π°Π½Π½ΡΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ, Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΡΠΌ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΌΠ΅ΡΠΎΠ΄ Π±ΠΈΠΎΡΠ΅ΠΌΠ΅Π΄ΠΈΠ°ΡΠΈΠΈ Ρ ΡΡΠ°ΡΡΠΈΠ΅ΠΌ ΠΌΠΈΠΊΡΠΎΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠΎΠ² — Π΄Π΅ΡΡΡΡΠΊΡΠΎΡΠΎΠ², ΠΊΠΎΡΠΎΡΡΠ΅ ΠΎΡΡΡΠ΅ΡΡΠ²Π»ΡΡΡ ΠΏΠΎΠ»Π½ΠΎΠ΅ Π΄Π΅Ρ Π»ΠΎΡΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ Ρ Π»ΠΎΡΠ°ΡΠΎΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΏΠΎΠ»Π»ΡΡΠ°Π½ΡΠΎΠ² Ρ ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ Π±Π΅Π·ΠΎΠΏΠ°ΡΠ½ΡΡ Π΄Π»Ρ ΠΎΠΊΡΡΠΆΠ°ΡΡΠ΅ΠΉ ΡΡΠ΅Π΄Ρ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ. ΠΠΎΡΡΠΎΠΌΡ ΠΈΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΠΏΡΡΠ΅ΠΉ Π±ΠΈΠΎΠ΄Π΅Π³ΡΠ°Π΄Π°ΡΠΈΠΈ Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠ² Π² Π½Π°ΡΡΠΎΡΡΠ΅Π΅ Π²ΡΠ΅ΠΌΡ Π²Π΅ΡΡΠΌΠ° Π°ΠΊΡΡΠ°Π»ΡΠ½ΠΎ.
Π‘ΠΎΡΡΠΎΡΠ½ΠΈΠ΅ Π²ΠΎΠΏΡΠΎΡΠ°. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ ΠΏΡΡΠ΅ΠΉ Π±ΠΈΠΎΠ΄Π΅Π³ΡΠ°Π΄Π°ΡΠΈΠΈ Ρ Π»ΠΎΡΠ°ΡΠΎΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ Π²Π΅Π΄ΡΡΡΡ ΠΈΠ½ΡΠ΅Π½ΡΠΈΠ²Π½ΠΎ Π²ΠΎ ΠΌΠ½ΠΎΠ³ΠΈΡ Π»Π°Π±ΠΎΡΠ°ΡΠΎΡΠΈΡΡ . ΠΡΠ΄Π΅Π»Π΅Π½ ΡΡΠ΄ Π°ΠΊΡΠΈΠ²Π½ΡΡ ΡΡΠ°ΠΌΠΌΠΎΠ² — Π΄Π΅ΡΡΡΡΠΊΡΠΎΡΠΎΠ², ΠΈΠ·ΡΡΠ΅Π½Ρ ΠΏΡΡΠΈ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΡ ΠΎΡΠ΄Π΅Π»ΡΠ½ΡΡ ΠΊΡΠ΅Π½ΠΎΠ±ΠΈΠΎΡΠΈΠΊΠΎΠ², ΠΎΡ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΠ·ΠΎΠ²Π°Π½Ρ ΡΠ΅ΡΠΌΠ΅Π½ΡΡ ΠΈ Π³Π΅Π½Ρ Π±ΠΈΠΎΠ΄Π΅Π³ΡΠ°Π΄Π°ΡΠΈΠ²Π½ΡΡ ΠΏΡΡΠ΅ΠΉ (Erb et al., 1998; Eulberg et al., 1998). ΠΠ·ΡΡΠ΅Π½Ρ ΠΏΡΡΠΈ Π΄Π΅Π³ΡΠ°Π΄Π°ΡΠΈΠΈ ΠΌΠΎΠ½ΠΎΡ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠ² ΠΈ ΠΌΠΎΠ½ΠΎΡ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠΎΠ² ΠΏΡΠ΅Π²Π΄ΠΎΠΌΠΎΠ½Π°Π΄Π°ΠΌΠΈ ΠΈ ΡΠΎΠ΄ΠΎΠΊΠΊΠΎΠΊΠ°ΠΌΠΈ (Hickey and Focht, 1990; Smith, 1990; Warhurst and Fewson, 1994; Zaitsev et al., 1995). ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ ΡΠ΅Π½ΠΎΠ» ΠΈ 2-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°Ρ, Π² ΠΎΡΠ½ΠΎΠ²Π½ΠΎΠΌ, ΠΎΠΊΠΈΡΠ»ΡΡΡΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΠΌΠΈ Π΄ΠΎ ΠΊΠ°ΡΠ΅Ρ ΠΎΠ»Π°, ΠΊΠΎΡΠΎΡΡΠΉ Π΄Π°Π»Π΅Π΅ ΡΡΠΈΠ»ΠΈΠ·ΠΈΡΡΠ΅ΡΡΡ ΠΏΠΎ ΠΌΠ΅ΡΠ°ΠΈΠ»ΠΈ ΠΎΡΡΠ°-ΠΏΡΡΠΈ. Π₯Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»Ρ, ΠΏΡΠΎΠ΄ΡΠΊΡΡ ΠΎΠΊΠΈΡΠ»Π΅Π½ΠΈΡ 3-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠ°, 3-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π°, 4-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π°, Π° Π² ΡΡΠ΄Π΅ ΡΠ»ΡΡΠ°Π΅Π² 2-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠ°, ΠΊΠ°ΠΊ ΠΏΡΠ°Π²ΠΈΠ»ΠΎ, ΡΠ°Π·Π»Π°Π³Π°ΡΡΡΡ ΡΠΎΠ»ΡΠΊΠΎ ΠΏΠΎ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΌΡ o/w/o-ΠΏΡΡΠΈ. Π-Π₯Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°Ρ ΠΌΠΎΠΆΠ΅Ρ ΡΠ°ΠΊΠΆΠ΅ ΡΠ°Π·Π»Π°Π³Π°ΡΡΡΡ ΠΏΠΎ ΠΏΡΠΎΡΠΎΠΊΠ°ΡΠ΅Ρ ΠΎΠ°ΡΠΈΠΎΠΌΡ ΠΏΡΡΠΈ ΠΊΠ°ΠΊ ΠΈ 4-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°Ρ. ΠΠ΄Π½Π°ΠΊΠΎ, Π΄Π°Π½Π½ΡΠ΅ ΠΎ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΠΈ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π°, Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ ΡΡΡΠΎΠΉΡΠΈΠ²ΠΎΠ³ΠΎ ΠΈΠ· Π²ΡΠ΅Ρ ΠΌΠΎΠ½ΠΎΡ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠ² ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΡ, ΡΡΠ°Π³ΠΌΠ΅Π½ΡΠ°ΡΠ½Ρ. ΠΡΠ΅Π΄ΠΏΠΎΠ»Π°Π³Π°Π΅ΡΡΡ, ΡΡΠΎ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ» ΠΌΠΎΠΆΠ΅Ρ ΡΡΠΈΠ»ΠΈΠ·ΠΈΡΠΎΠ²Π°ΡΡΡΡ ΠΡΠ°ΠΌ-ΠΎΡΡΠΈΡΠ°ΡΠ΅Π»ΡΠ½ΡΠΌΠΈ Π±Π°ΠΊΡΠ΅ΡΠΈΡΠΌΠΈ ΠΏΠΎ Π°Π½Π°Π»ΠΎΠ³ΠΈΠΈ Ρ 2-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠΎΠΌ Π»ΠΈΠ±ΠΎ ΡΠ΅ΡΠ΅Π· ΠΊΠ°ΡΠ΅Ρ ΠΎΠ» ΠΏΠΎ ΠΎΠ±ΡΡΠ½ΠΎΠΌΡ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ, Π»ΠΈΠ±ΠΎ ΡΠ΅ΡΠ΅Π· 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» ΠΏΠΎ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΌΡ. Π Π°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΠ΅ ΡΡΠΈΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ ΠΡΠ°ΠΌ-ΠΏΠΎΠ»ΠΎΠΆΠΈΡΠ΅Π»ΡΠ½ΡΠΌΠΈ Π±Π°ΠΊΡΠ΅ΡΠΈΡΠΌΠΈ Π΄Π΅ΡΠ°Π»ΡΠ½ΠΎ Π½Π΅ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π»ΠΎΡΡ.
Π¦Π΅Π»Ρ ΠΈ Π·Π°Π΄Π°ΡΠΈ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ
Π¦Π΅Π»ΡΡ ΡΠ°Π±ΠΎΡΡ, Π±ΡΠ»ΠΎ ΠΈΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΡΠ½Π·ΠΈΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΈ Π³Π΅Π½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΡ Π°ΡΠΏΠ΅ΠΊΡΠΎΠ² 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΡΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ Ρ Rhodococcus opacus 1Π‘Π , ΡΡΠΈΠ»ΠΈΠ·ΠΈΡΡΡΡΠ΅Π³ ΠΎ 4-Ρ Π»ΠΎΡ ΠΈ 2,4-Π΄ΠΈΡ Π»ΠΎΡΡΠ΅Π½ΠΎΠ».
ΠΠ»Ρ Π΄ΠΎΡΡΠΈΠΆΠ΅Π½ΠΈΡ ΡΡΠΎΠΉ ΡΠ΅Π»ΠΈ Π±ΡΠ»ΠΈ ΠΏΠΎΡΡΠ°Π²Π»Π΅Π½Ρ ΡΠ»Π΅Π΄ΡΡΡΠΈΠ΅ Π·Π°Π΄Π°ΡΠΈ:
1. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ Π²Π°ΡΠΈΠ°Π½ΡΠΎΠ² R. opacus 1Π‘Π , ΡΠ°ΡΡΡΡΠΈΡ Π½Π° 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π΅, 3-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π΅ ΠΈ 3-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠ΅.
2. ΠΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΠΏΡΡΠΈ Π΄Π΅Π³ΡΠ°Π΄Π°ΡΠΈΠΈ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π° ΠΈ Π΄ΠΎΠΊΠ°Π·Π°ΡΠ΅Π»ΡΡΡΠ²ΠΎ ΡΡΠ½ΠΊΡΠΈΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΡ ΡΡΠΎΠ³ΠΎ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΡ.
3. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅, ΠΎΡΠΈΡΡΠΊΠ°, Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΡΡΠΈΠΊΠ° ΠΊΠ»ΡΡΠ΅Π²ΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ² 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ.
4. ΠΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΈ ΡΠ΅ΠΊΠ²Π΅Π½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ Π³Π΅Π½ΠΎΠ² 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ Ρ R. opacus 1Π‘Π , Π²ΡΡΠ°ΡΠ΅Π½Π½ΠΎΠ³ΠΎ Π½Π° 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π΅.
5. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ ΡΡΠ½ΠΊΡΠΈΠΉ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ² Π½ΠΎΠ²ΠΎΠ³ΠΎ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠΌ.
ΠΠ°ΡΡΠ½Π°Ρ Π½ΠΎΠ²ΠΈΠ·Π½Π°. ΠΠΎΠ»ΡΡΠ΅Π½Ρ Π²Π°ΡΠΈΠ°Π½ΡΡ Rhodococcus opacus 1 CP, ΡΠ°ΡΡΡΡΠΈΠ΅ Π½Π° ΡΡΠ΅Π΄Π°Ρ Ρ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠΌ, 3-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠΌ ΠΈ Π-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠΎΠΌ. ΠΡΠ΄Π΅Π»Π΅Π½Ρ ΠΈ ΠΎΡ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΠ·ΠΎΠ²Π°Π½Ρ ΡΠ΅ΡΠΌΠ΅Π½ΡΡ 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΡ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π° R. opacus 1Π‘Π : Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Π°, Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ ΡΠΈΠΊΠ»ΠΎΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π°, Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π° ΠΈ Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Π°. ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Π² 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ Ρ ΠΡΠ°ΠΌ-ΠΏΠΎΠ»ΠΎΠΆΠΈΡΠ΅Π»ΡΠ½ΠΎΠ³ΠΎ ΡΡΠ°ΠΌΠΌΠ° ΠΏΡΠΈΠ½ΠΈΠΌΠ°Π΅Ρ ΡΡΠ°ΡΡΠΈΠ΅ Ρ Π»ΠΎΡΠΌΡΠΊΠ¬Π½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π°, Π°Π½Π°Π»ΠΎΠ³ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ° ΠΊΠ»Π°ΡΡΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΎΡΠΏΡ-ΠΏΡΡΠΈ, Π½Π΅ ΡΡΠ½ΠΊΡΠΈΠΎΠ½ΠΈΡΡΡΡΠΈΠΉ Π² 4-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΡΡΠΎΠ³ΠΎ ΠΆΠ΅ ΡΡΠ°ΠΌΠΌΠ° ΠΈ Π² 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΡΠ°ΠΌ-ΠΎΡΡΠΈΡΠ°ΡΠ΅Π»ΡΠ½ΡΡ ΡΡΠ°ΠΌΠΌΠΎΠ². Π£ΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΎ, ΡΡΠΎ Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Π° Π½ΠΎΠ²ΠΎΠ³ΠΎ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ ΠΎΠ±Π»Π°Π΄Π°Π΅Ρ ΡΠΈΡΠΎΠΊΠΎΠΉ ΡΡΠ±ΡΡΡΠ°ΡΠ½ΠΎΠΉ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ½ΠΎΡΡΡΡ ΠΈ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎ ΡΠ°Π·Π»Π°Π³Π°Π΅Ρ 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ». ΠΠΎΠΊΠ°Π·Π°Π½Π° ΡΠ·ΠΊΠ°Ρ ΡΡΠ±ΡΡΡΠ°ΡΠ½Π°Ρ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ½ΠΎΡΡΡ Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ ΡΠΈΠΊΠ»ΠΎΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Ρ, ΡΡΠ±ΡΡΡΠ°ΡΠ°ΠΌΠΈ ΠΊΠΎΡΠΎΡΠΎΠΉ ΡΠ²Π»ΡΡΡΡΡ 2-Π·Π°ΠΌΠ΅ΡΠ΅Π½Π½ΡΠ΅ ΠΌΡΠΊΠΎΠ½Π°ΡΡ. Π€Π΅ΡΠΌΠ΅Π½Ρ ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅Ρ ΡΠ΅Π°ΠΊΡΠΈΡ ΡΠΎΠ»ΡΠΊΠΎ Ρ ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΠ³ΠΎΠ½Π°, Π½ΠΎ Π½Π΅ ΠΎΡΡΡΠ΅ΡΡΠ²Π»ΡΠ΅Ρ Π΅Π³ΠΎ Π΄Π΅Ρ Π»ΠΎΡΠΈΡΠΎΠ²Π°Π½ΠΈΡ. Π₯Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π° Π΄Π΅Π³Π°Π»ΠΎΠ³Π΅Π½ΠΈΡΡΠ΅Ρ 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ Ρ ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ ////ΠΎΠ΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½Π°. ΠΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Π° 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ½Π° ΠΏΠΎ ΠΎΡΠ½ΠΎΡΠ΅Π½ΠΈΡ ΠΊ ΡΠΈΡ-Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½Ρ, mpauc-j\mΠ»Π°ΠΊΡΠΎ11 Π½Π΅ ΡΠ²Π»ΡΠ΅ΡΡΡ ΡΡΠ±ΡΡΡΠ°ΡΠΎΠΌ ΡΡΠΎΠ³ΠΎ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°. ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½ΠΎ ΡΠ°ΡΠΏΠΎΠ»ΠΎΠΆΠ΅Π½ΠΈΠ΅ Π³Π΅Π½ΠΎΠ² 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠ³ΠΎ ΠΎΠΏΠ΅ΡΠΎΠ½Π° ΠΡΠ°ΠΌ-ΠΏΠΎΠ»ΠΎΠΆΠΈΡΠ΅Π»ΡΠ½ΠΎΠ³ΠΎ ΡΡΠ°ΠΌΠΌΠ°, ΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠ΅Π³ΠΎ Π³Π΅Π½Ρ Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Ρ, Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Ρ, Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ ΡΠΈΠΊΠ»ΠΎΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Ρ, Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Ρ ΠΈ ΡΠ΅Π³ΡΠ»ΡΡΠΎΡΠ½ΠΎΠ³ΠΎ Π±Π΅Π»ΠΊΠ°. ΠΠΎΠ»ΡΡΠ΅Π½Π° ΠΏΠΎΠ»Π½Π°Ρ Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄Π½Π°Ρ ΠΏΠΎΡΠ»Π΅Π΄ΠΎΠ²Π°ΡΠ΅Π»ΡΠ½ΠΎΡΡΡ ΡΡΠΈΡ Π³Π΅Π½ΠΎΠ² (Π³Π΅Π½Π° ΡΠ΅Π³ΡΠ»ΡΡΠΎΡΠ½ΠΎΠ³ΠΎ Π±Π΅Π»ΠΊΠ° ΡΠ°ΡΡΠΈΡΠ½ΠΎ).
ΠΡΠ°ΠΊΡΠΈΡΠ΅ΡΠΊΠΎΠ΅ Π·Π½Π°ΡΠ΅Π½ΠΈΠ΅ ΡΠ°Π±ΠΎΡΡ. R. opacus ICP, ΡΡΠΈΠ»ΠΈΠ·ΠΈΡΡΡΡΠΈΠΉ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»., ΠΌΠΎΠΆΠ΅Ρ ΠΈΡΠΏΠΎΠ»ΡΠ·ΠΎΠ²Π°ΡΡΡΡ Π΄Π»Ρ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΡ ΡΡΠΎΠ³ΠΎ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΡ ΠΊΠ°ΠΊ Π² Π±ΠΈΠΎΡΠ΅Π°ΠΊΡΠΎΡΠ°Ρ , ΡΠ°ΠΊ ΠΈ Π² 7 Π΅ΡΡΠ΅ΡΡΠ²Π΅Π½Π½ΠΎΠΉ ΡΡΠ΅Π΄Π΅. Π Π°Π·ΡΠ°Π±ΠΎΡΠΊΠ° ΠΌΠ΅ΡΠΎΠ΄Π° Π°Π΄Π°ΠΏΡΠ°ΡΠΈΠΈ R. opacus 1Π‘Π ΠΊ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Ρ, Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎ, ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΡ ΠΏΠΎΠ»ΡΡΠΈΡΡ ΡΠΎΡΡ ΠΈ Π΄ΡΡΠ³ΠΈΡ ΡΡΠ°ΠΌΠΌΠΎΠ² ΡΡΠΎΠ³ΠΎ ΡΠΎΠ΄Π° Π½Π° ΡΡΠ΅Π΄Π°Ρ Ρ ΡΠ°Π·Π»ΠΈΡΠ½ΡΠΌΠΈ ΠΊΡΠ΅Π½ΠΎΠ±ΠΈΠΎΡΠΈΠΊΠ°ΠΌΠΈ. ΠΠ°Π½Π½ΡΠ΅ ΠΎΠ± ΠΎΡΠ³Π°Π½ΠΈΠ·Π°ΡΠΈΠΈ ΠΊΠ°ΡΠ°Π±ΠΎΠ»ΠΈΡΠ½ΡΡ ΠΎΠΏΠ΅ΡΠΎΠ½ΠΎΠ² Π½Π΅ΠΎΠ±Ρ ΠΎΠ΄ΠΈΠΌΡ Π΄Π»Ρ ΠΊΠΎΠ½ΡΡΡΡΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΡΡ ΡΡΠ°ΠΌΠΌΠΎΠ² — Π΄Π΅ΡΡΡΡΠΊΡΠΎΡΠΎΠ² ΠΌΠ΅ΡΠΎΠ΄Π°ΠΌΠΈ Π³Π΅Π½Π½ΠΎΠΉ ΠΈΠ½ΠΆΠ΅Π½Π΅ΡΠΈΠΈ.
ΠΠΠΠΠ ΠΠΠ’ΠΠ ΠΠ’Π£Π Π«.
Π²ΡΠ²ΠΎΠ΄Ρ.
1. ΠΠΎΠ»ΡΡΠ΅Π½Ρ Π²Π°ΡΠΈΠ°Π½ΡΡ Rhodococcus opacus 1Π‘Π , Π΄Π΅ΡΡΡΡΠΊΡΠΎΡΠ° 4-Ρ Π»ΠΎΡ ΠΈ 2,4-Π΄ΠΈΡ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π°, ΡΠΏΠΎΡΠΎΠ±Π½ΡΠ΅ ΡΠ°ΡΡΠΈ Π½Π° 3-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π΅, 3-Ρ Π»ΠΎΡΠ±Π΅Π½Π·ΠΎΠ°ΡΠ΅ ΠΈ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π΅.
2. .ΠΠ° ΠΎΡΠ½ΠΎΠ²Π°Π½ΠΈΠΈ Ρ ΡΠΎΠΌΠ°ΡΠΎΠ³ΡΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΈ ΠΌΠ°ΡΡ-ΡΠΏΠ΅ΠΊΡΡΠΎΠΌΠ΅ΡΡΠΈΡΠ΅ΡΠΊΠ½Ρ Π΄Π°Π½Π½ΡΡ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ.
2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ» ΡΠ°Π·Π»Π°Π³Π°Π΅ΡΡΡ R. opacus 1Π‘Π ΡΠ΅ΡΠ΅Π· 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ», 2-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ, 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈ ?/?/Ρ-Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½.
3. ΠΡΠΈΡΠ΅Π½Ρ ΠΈ ΠΎΡ Π°ΡΠ°ΠΊΡΠ΅ΡΠΈΠ·ΠΎΠ²Π°Π½Ρ ΡΠ΅ΡΠΌΠ΅Π½ΡΡ ΠΏΡΠ΅Π²ΡΠ°ΡΠ΅Π½ΠΈΡ 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»Π° opacus 1 CP:
3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ» 1,2-Π΄ΠΈΠΎΠΊΡΠΈΠ³Π΅Π½Π°Π·Π°, 2-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½Π°Ρ ΡΠΈΠΊΠ»ΠΎΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π°, 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π° ΠΈ Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Π°.
4. ΠΠ΅ΡΠΎΠ΄ΠΎΠΌ 19F-^MP ΠΏΠΎΠ΄ΡΠ²Π΅ΡΠΆΠ΄Π΅Π½Π° ΡΡΠ½ΠΊΡΠΈΡ ΠΊΠ°ΠΆΠ΄ΠΎΠ³ΠΎ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ° 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΡΠΎ-ΠΏΡΡΠΈ R. opacus 1 Π‘Π . ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ 5-Ρ Π»ΠΎΡΠΌΡΠΊΠΎΠ½ΠΎΠ»Π°ΠΊΡΠΎΠ½ ΠΈΠ·ΠΎΠΌΠ΅ΡΠ°Π·Π° ΠΎΡΡΡΠ΅ΡΡΠ²Π»ΡΠ΅Ρ Π΄Π΅Π³Π°Π»ΠΎΠ³Π΅ΠΈΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ Π³Π°Π»ΠΎΠΌΡΠΊΠΎΠ½Π°ΡΠΎΠ² Ρ ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ Π³/Π½Π±-Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½Π°.
5. ΠΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½Ρ ΠΈ ΡΠ΅ΠΊΠ²Π΅Π½ΠΈΡΠΎΠ²Π°Π½Ρ Π³Π΅Π½Ρ, ΠΊΠΎΠ΄ΠΈΡΡΡΡΠΈΠ΅ ΡΠ΅ΡΠΌΠ΅Π½ΡΡ 3-Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΠΎΠΉ Π²Π΅ΡΠ²ΠΈ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠ³ΠΎ ΠΎΡΠΏΡ-ΠΏΡΡΠΈ R. opacus 1Π‘Π . ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ ΠΎΠ½ΠΈ ΡΠΎΡΡΠ°Π²Π»ΡΡΡ Π΅Π΄ΠΈΠ½ΡΠΉ ΠΎΠΏΠ΅ΡΠΎΠ½, ΠΎΡΠ»ΠΈΡΠ°ΡΡΠΈΠΉΡΡ ΠΎΡ Π΄ΡΡΠ³ΠΈΡ ΠΈΠ·Π²Π΅ΡΡΠ½ΡΡ ΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΡΡ ΠΈ Ρ Π»ΠΎΡΠΊΠ°ΡΠ΅Ρ ΠΎΠ»ΡΠ½ΡΡ ΠΎΠΏΠ΅ΡΠΎΠ½ΠΎΠ².
6. ΠΠ° ΠΎΡΠ½ΠΎΠ²Π°Π½ΠΈΠΈ Π°Π½Π°Π»ΠΈΠ·Π° ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠΎΠ² ΡΠ½Π·Π½ΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΈΡ , ΡΠΏΠ΅ΠΊΡΡΠ°Π»ΡΠ½ΡΡ ΠΈ Π³Π΅ΠΏΠ΅Π³ΠΈΡΠ΅ΡΠΊΠΏΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠΉ ΠΏΡΠ΅Π΄Π»ΠΎΠΆΠ΅Π½ Π½ΠΎΠ²ΡΠΉ ΠΌΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ ΠΎΡΠΏΡ-ΠΏΡΡΡ ΡΠ°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΡ 2-Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π° R. opacus 1 Π‘Π .
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- ΠΠΎΡΠ»Π°ΡΠΎΠ² Π‘.Π., ΠΠ°Π»ΡΡΠ΅Π²Π° Π. Π., Π¨Π΅Π²ΡΠ΅Π½ΠΊΠΎ Π. Π., ΠΠΎΠ»ΠΎΠ²Π»Π΅Π²Π° Π. Π. 1989. Π Π°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΠ΅ Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠ² ΠΊΡΠ»ΡΡΡΡΠΎΠΉ Rhodococcus erythropolis. ΠΠΈΠΊΡΠΎΠ±ΠΈΠΎΠ»ΠΎΠ³ΠΈΡ, Ρ. 58, Π΅Π΅. 802−806.
- ΠΠ°Π±ΠΎΡΠΈΠ½Π° Π.Π., ΠΠ°ΡΡΡΠ½ΠΈΠΊΠΎΠ²Π° Π. Π., ΠΠ°ΡΠΊΡΠ½ΠΎΠ² Π. Π., ΠΠΎΠ»ΠΎΠ²Π»Π΅Π² Π Π., ΠΠΎΠ»ΠΎΠ²Π»Π΅Π²Π° Π. Π. 1997. Π Π°Π·Π»ΠΎΠΆΠ΅Π½ΠΈΠ΅ ΠΏΠ΅Π½ΡΠ°Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»Π° Π² ΠΏΠΎΡΠ²Π΅ ΠΈΠ½ΡΡΠ°Π΄ΡΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΌ ΡΡΠ°ΠΌΠΌΠΎΠΌ Streptomyces rochei 303 ΠΈ Π°ΠΊΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΉ ΠΏΠΎΡΠ²Π΅Π½Π½ΠΎΠΉ ΠΌΠΈΠΊΡΠΎΡΠ»ΠΎΡΠΎΠΉ. ΠΠΈΠΊΡΠΎΠ±ΠΈΠΎΠ»ΠΎΠ³ΠΈΡ, Ρ. 66, ΡΠ΅. 661−666.
- ΠΠ°Π»ΡΡΠ΅Π²Π° Π.Π., Π‘ΠΎΠ»ΡΠ½ΠΈΠΊΠΎΠ²Π° Π. Π., ΠΠΎΠ»ΠΎΠ²Π»Π΅Π²Π° Π. Π. 1991. ΠΠΈΡΠΎΠΊΠ°ΡΠ΅Ρ Π°Π·Ρ ΡΡΠ°ΠΌΠΌΠ° Rhodococcus erythropolis Π΄Π΅ΡΡΡΡΠΊΡΠΎΡΠ° Ρ Π»ΠΎΡΡΠ΅Π½ΠΎΠ»ΠΎΠ²: ΠΎΡΠΈΡΡΠΊΠ° ΠΈ ΡΠ²ΠΎΠΉΡΡΠ²Π°. ΠΠΈΠΎΡ ΠΈΠΌΠΈΡ, Ρ. 56, ΡΡ. 2188−2*197.
- Π‘ΠΎΠ»ΡΠ½ΠΈΠΊΠΎΠ²Π° Π.Π., ΠΠ°Π»ΡΡΠ΅Π²Π° Π. Π., ΠΠΎΠ»ΠΎΠ²Π»Π΅Π²Π° Π. Π. 1995. ΠΠΎΠ΄ΠΈΡΠΈΡΠΈΡΠΎΠ²Π°Π½Π½ΡΠΉ ΠΎΡΡΠΎ-ΠΏΡΡΡ Ρ ΡΡΠ°ΠΌΠΌΠ° Pseudomonas putida 87. ΠΎΡΠΈΡΡΠΊΠ° ΠΈ ΡΠ²ΠΎΠΉΡΡΠ²Π° Π΄ΠΈΠ΅Π½Π»Π°ΠΊΡΠΎΠ½ Π³ΠΈΠ΄ΡΠΎΠ»Π°Π·Ρ. 1>ΠΏΠΎΡ ΠΈΠΌΠΈΡ, Ρ. 60, ΡΡ. 1251−1260.
- Π’ΡΠ°Π²ΠΊΠΈΠ½ Π.Π., ΠΠΈΠ½ΡΠΊΠΎ Π. Π., ΠΠΎΠ»ΠΎΠ²Π»Π΅Π²Π° Π. Π. 1999. ΠΡΠΈΡΡΠΊΠ° ΠΈ ΡΠ²ΠΎΠΉΡΡΠ²Π° ΠΌΠ°Π»Π΅ΠΈΠ»Π°ΡΠ΅ΡΠ°Ρ ΡΠ΅Π΄ΡΠΊΡΠ°Π·Ρ ΠΈΠ· ΡΡΠ°ΠΌΠΌΠ° Nocardioses simplex ΠΠ, ΡΡΠΈΠ»ΠΈΠ·ΠΈΡΡΡΡΠ΅Π³ΠΎ ΡΠ΅Π½ΠΎΠΊΡΠΈΠ°Π»ΠΊΠ°Π½ΠΎΠ²ΡΠ΅ Π³Π΅ΡΠ±ΠΈΡΠΈΠ΄Ρ 2,4-Π ΠΈ 2,4,5-Π’. ΠΠΈΠΎΡ ΠΈΠΌΠΈΡ, Ρ.64, ΡΡ. 751−757.
- Alting-Mees Π.Π., Sorge J.A., Short J. M. 1992. pBluescriptll. multifunctional cloning and mapping vectors. Methods Enzymol., v. 216, pp. 483−410.
- Aoki K., Uemori Π’., Shinke R., Nishira H. 1985. Further characterization of bacterial production of anthranilic acid from aniline. Agric. Biol. Chem., v. 49, pp. 1151−1158.
- Apajalahti J.H.A., Salkinoja-Salonen M.S. 1986. Degradation of polychlorinated phenols by Rhodococcus chlorophenolicus. Appl. Microbiol. Biotechnol., v. 25, pp. 62−67.
- Arensdorf J.I., Focht D.D. 1995. A meta cleavage pathway for 4-chlorobenzoate, an intermediate in the metabolism of 4-chlorobiphenyl by Pseudomonas cepacia P I 66. Appl. Environ. Microbiol., v. 61, pp. 443−447.
- Asturias J.A., Eltis L.D., Prucha M., Timmis K.N. 1994. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus gloheriiliis P6: identification of a new family of extradiol dioxygenases. J. Biol. Chem., v. 269, pp. 7807−7815
- Avigad G, Englard S" Olsen B.R., Wolfenstein-Todel C., Wiggins R. 1974. Molecular properties of c/.v.c/v-muconate cycloisomerase from Pseudomonas putida. J. Mol. Biol., v. 89, pp. 651−662.
- Banerni S.K., Wei M., Bajpai R.K. 1993 Pentachlorophenol interactions with soil. Water
- Air Soil Pollut., v. 69, pp. 149 -163.
- Battels I., Knackmuss H.-J., Reineke W. 1984. Suicide inactivation of catechol 2,3-dioxygenase from Pseudomonas putida mt-2 by 3-halocatechols. Appl. Environ. Microbiol., v. 47, pp: 500−505.
- Beadle C.A., Smith A.R.W. 1982. The purification and properties of 2,4-dichlorophenol hydroxylase from a strain of Acinetobacter species. Eur. J. Biochem., v. 123, pp. 323−332.
- Bethesda Research Laboratories. 1986. BRL pUC host: Π coli DH5a competent cells. Bethesda Res. Lab. Focus, 8, 2, p. 9.
- Beveridge A.J., Ollis D.L. 1995. A theoretical study of substrate-induced activation of dienelactone hydrolase. Protein Engineering, v. 8, pp. 135−142.
- Blasco R., Wittich R.-M., Mallavarapu M., Timmis K. N., Pieper D.H. 1995. From xenobiotic to antibiotic, formation of protoanemonin from 4-chlorocatechol by enzymes of the 3-oxoadipate pathway. J. Biol. Chem., v. 270, pp. 29 229−29 235.
- Boersma M.G., Solyanikova I., van Berkel W.J.H., Vervoort J., Golovleva L., Rietjens I.M.C.M. 2000. i9 °F NMR metabolomics for the elucidation of microbial degradation pathways of fluorophenols. J. Ind. Microbiol. Biotechnol., v. 24, pp. 1−13.
- Boldt Y.R., Sadowsky M.J., Ellis L.B.M., Que L., JR., Wackett L P. 1995. A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family. J. Bacteriol., v. 177, pp. 1225−1232.
- Bollag J.-M. 1992 Decontaminating soil with enzymes. Environ. Sci. Technol., v. 26, pp. 1876−1881.
- Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anai. Biochem., v. 72, pp. 248−254.
- Broderick J.B., O’Halloran T.V. 1991. Overproduction, purification and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance. Biochemistry, v. 30, pp. 7349−7358.
- Bruce N., Cain R. 1990. Hydroaromatic metabolism in Rhodococcus rhodochrous: purification and characterization of its NAD-dependent quinate dehydrogenase. Arch. Microbiol., v. 154,$). 179−186.
- Bruce N.C., Cain R.B. 1988. Π-methylmuconolactone, a key intermediate in the dissimilation of methylaromatic compounds by a modified 3-oxoadipate pathway evolved in nocardioform actinomycetes. FEMS Microbiol. Lett., v. 50, pp. 233−239.
- Cain R.B. 1981. Regulation of aromatic and hydroaromatic catabolic pathways in nocardioform actinomycetes, Schaal/pulverer (eds): Actinomycetes, Zbl. Bart. Suppl. 11. Gustav Fischer Verlag. Stuttgart. New York.
- Catelani D., Fiecchi A., GalliE. 1971. (+)-y-carboxymethyl-y-methyl-Aa-butenolide: a 1,2-ring-fission product of 4-methylcatechol by Pseudomonas desmolyticum. Biochem. J., v. 121, pp. 89−92.
- Cha C.-J. 2001. Biological production of optically active muconolactones by Rhodococcus rhodochrous. Appl. Microbiol. Biotechnol., v. 56, pp. 453−457.i
- Cha C-J., Cain R.B., Bruce N.C. 1998. The modified /?-ketoadipate pathway in Rhodococcus rhodochrous N75: enzymology of 3-methylmuconolactone metabolism. J. Bacteriol., v. 180, pp. 6668−6673.
- Chari R.V.J., Whitman C.P., Kozarich J.W. 1987b. Absolute stereochemical course of muconolactone Π-vsomerase and of 4-carboxymuconolactone decarboxylase: a! H NMR «ricochet» analysis. J. Am. Chem. Soc., v. 109, pp. 5520−5521.
- Chatteijee D.K., Kellogg S.T., Hamada S., Chakrabarty A.M. 1981. Plasmid specifying total degradation of 3-chlorobenzoate by a modified or/ho pathway. J. Bacteriol., v. 146, pp. 639−646.
- Cheah E., Austin C., Ashley G.W., Ollis D. 1993. Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occurring Cys-His-Asp triad. Protein Engineering, v. 6, pp. 575−583.
- Chugani S.A., Parsek M.R., Chakrabarty A.M. 1998. Transcriptional repression mediated by a LysR-type regulator CatR bound at multiple binding sites. J. Bacteriol., v. 180, pp. 2367−2372.
- Chugani S.A., Parsek MR., Hershberger C.D., Murakami K., Ishihama A., Chakrabarty A.M. 1997. Activation of the catBCA promoter: probing the interaction of CatR and RNA polymerase through in vitro transcription. J. Bacteriol., v. 179, pp. 2221−2227.
- Coco W.M., Parsek M.R., Chakrabarty A.M. 1994. Purification of the LysR family regulator, ClcR, and its interaction with the Pseudomonas putida clcABC chlorocatechol operon promoter. J. Bacteriol., v. 176, pp. 5530−5533.
- Cole J R., Cascarelli A.L., Mohn W.W., Tiedje J.M. 1994. Isolation and characterization of a novel bacterium growing via reductive dehalogenation of 2-chlorophenol. Appl. Environ. Microbiol, v. 60, pp. 3536−3542.
- Cook A. M., Hutter R. 1986. Ring dechlorination of deethylsimazine by hydrolases from a Rhodococcus corallinus. FEMS Microbiol. Lett., v. 34, pp. 335−338.
- Copley S.D., 2000. Evolution of a metabolic pathway for degradation of a toxic xenobiotic: the patchwork approach. TIBS, v. 25, pp. 261−265.
- Detmer K., Massey 'V. 1984. Effect of monovalent anions on the mechanism of phenol ' hydroxylase. J. Biol.- Chem., v. 259, pp. 11 265−11 272.
- Diezel W., Kopperschlager G., Hofmann E. 1972. An improved procedure for protein staining in polyacrylamide gels with a new type of Coomassie Brilliant Blue. Analyt. Biochem., v. 48, pp. 617−620.
- Dixon M. 1953. The determination of enzyme inhibitor constants. Biochem. J., v. 55, pp. 170−171.
- Dorn E., Knackmuss H.-J. 1978a. Chemical structure and biodegradability of halogenated aromatic compounds. Two catechol 1,2-dioxygenases from a 3-chlorobenzoate grown pseudomonad. Biochem. J., v. 174, pp. 73−84.
- Dorn E., Knackmuss H.-J. 1978b. Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol. Biochem. J., v. 174, pp. 85−94.
- Eltis L.D., Bolin J.T. 1996. Evolutionary relationships among extradiol dioxygenases. J. Bacteriol., v. 178, pp. 5930−5937.
- Erb R.W., Timmis K.N., Rieper D.H. 1998. Characterization of a gene cluster from Ralstonia eutropha JMPI34 encoding metabolism of 4-methylmuconolactone. Gene, v. 206, pp. 53−62.
- Eulberg D., Golovleva L.A., Schlomann M. 1997. Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP. J. Bacteriol., v. 179, pp. 370−381.
- Fersht A. 1985. Enzyme structure and mechanism, 2nd ed., W.H. Freeman and Co., New York.
- Fetzner S., Lingens F. 1994. Bacterial dehalogenases: biochemistry, genetics, and biotechnological applications. Microbiol. Rev., v.58, pp. 641−685.
- Finnerty W.R. 1992. The biology and genetics of the genus Rhodococcus. Ann. Rev. Microbiol., v. 46, pp. 193−218.
- Frantz Π., Chakrabarty A.M. 1987. Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation. Proc. Natl. Acad. Sci. USA, v. 84, pp. 4460−4464.
- Frantz Π., Ngai K.-E., Chatteijee D.K., Ornston L.N., Chakrabarty A.M. 1987. Nucleotide sequence and expression of clcD, a plasmid-borne dienelactone hydrolase gene from Pseudomonas sp. strain Π13. J. Bacteriol., v. 169, pp. 704−709.
- Fujiwara M., Golovleva L.A., Saeki Y., Nozaki M., Hayaishi O. 1975. Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a pseudomonad. J. Biol. Chem., v. 250, pp. 4848−4855.
- Funabiki Π’., Inoue Π’., Kojima H., Konishi Π’., Tanaka Π’., Yoshida S. 1990. Extended-Hvickel study on oxygen insertion into the aromatic ring by model complexes for catechol dioxygenases. J. Mol. Catal., v. 59, pp. 367−371.
- Gaal A.B., Neujahr H.Y. 1980. Maleylacetate reductase from Trichosporon cutaneum. Biochem J., v. 185, pp. 783−786.
- Gerlt J.A., Gassman P.G. 1992. Understanding enzyme-catalyzed proton abstraction from carbon acids: details of stepwise mechanisms for /^-elimination reactions. J. Am. Chem. Soc., v. 114, pp. 5928−5934.
- Ghosal d., You I.-S., Chatteijee D.K., Chakrabarty A.M. 1985. Genes specifying degradation of 3-chlorobenzoic acid in plasmids pAC27 and pJP4. Proc. Natl. Acad. Sci. USA, v. 82, pp. 1638−1642.
- Gibson D.T. 1987. Microbial metabolism of aromatic hydrocarbons and the carbon cycle, pp. 33−58. In Hagedorn S.R., Hanson R.S., Kunz D.A. (ed.), Microbial metabolism and the carbon cycle. Harwopd academic publishers, Chur, Switzerland.
- Gorlatov S.N., Golovleva L.A. 1992. Effect of cosubstrates on the dechlorination of selected chlorophenolic compounds by Rhodococcns erythropolis 1CP. J. Basic Microbiol., v.32, pp. 177−184.
- Goulding C., Gillen C. J., Bolton E. 1988. Biodegradation of substituted benzenes. J. Appl. Bacterid., v. 65, pp. 1−5.
- Gribble G.W. 1994. The natural production of chlorinated compounds. Environ. Sci.
- Technol., v. 28, pp. 310A-319A.
- Hftggblom M.M. 1990. Mechanisms of bacterial degradation and transformation of chlorinated monoaromatic compounds. J. Basic Microbiol., v. 30, pp. 115−141.
- Haggblom M.M. 1992. Microbial breakdown of halogenated aromatic pesticides and related compounds. FEMS Microbiol. Rev., v. 103, pp. 28−72.
- Haggblom M.M., Janke D" Middeldorp P.M.J., Salkinoja-Salonen M.S. 1989a. O-methylation of chlorinated phenols in the genus Rhodococcns. Arch. Microbiol., v. 152, pp. 6−9. ,
- Haggblom M.M., Janke D., Salkinoja-Salonen M.S. 1989b. Transformation of chlorinated phenolic compounds in the genus Rhodococcus. Microbiol. Ecol., v. 18, pp. 147−159.
- Haggblom M.M., Nohynek L.J., Salkinoja-Salonen M.S. 1988. Degradation and O-methylation of chlorinated phenolic compounds by Rhodococcus and Mycobacterium strains. Appl. Environ. Microbiol., v. 54, pp. 3043−3052.
- Haigler B E., Johnson G.R., Suen W.-C., Spain J.C. 1999. Biochemical and genetic evidence for meta-ΠΏΡ cleavage of 2,4,5-trihydroxytoluene in Burkholderia sp. strain DNT. J. Bacteriol., v. 181, pp. 965−972.
- Hammer A., Hildenbrand Π’., Hoier H, Ngai K.-L., Schlomann M., Stezowski J.J. 1993. Crystallization and preliminary, X-ray data of chloromuconate cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4). J. Mol. Biol., v. 232, pp. 305−307.
- Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T. 1995. Ciystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science, v. 270, pp. 976−980.
- Harayama S., Rekik M. 1989. Bacterial aromatic ring-cleavage enzymes are classified in two different gene families. J. Biol. Chem., v. 264, pp. 15 328−15 333.
- Hayaishi O. 1969. Nature and mechanism of oxygenases. Science, v. 164, pp. 389−396.
- Heiss G., Stolz A., Kuhm A.E., Mtiller K., Klein J., Altenbuchner J., Knackmuss K.-J. 1995. Characterization of a 2,3-dihydroxybiphenyl dioxygenase from the naphthalenesulfonate-degrading bacterium strain BN6. J. Bacteriol., v. 177, pp. 5865−5871.
- Heiss G., Muller C., Altenbuchner J., Stolz A. 1997. Analysis of a new dimeric extradiol dioxygenase from a naphthalenesulfonate-degrading sphingomonad. Microbiology, v. 143, pp. 1691−1699.
- Held M., Suske W., Schmid A., Engesser K.-H., Kohler H.-P.E., Witholt B" Wubbolts M.G. 1998. Preparative scale production of 3-substituted catechols using a novel monooxygenase from Pseudomonas azelaica HBP1. J. Mol. Cat. B: enzymatic, v. 5, pp. 87−93.
- Helin S., Kahn P.C., Guha B.L., Mallows D.G., Goldmann A. 1995. The refined X-ray structure of muconate lactonizing enzyme from Pseudomonas putida PRS2000 at 1.85 A resolution. J. Mol. Biol., v. 254, pp. 918−941.
- Hensel J., Straube G. 1990. Kinetic studies of phenol degradation by Rhodococcus sp. PI. II. Continuous cultivation. Antonie van Leeuwenhoek J. Microbiol. Ser., v. 57, pp. 33−36.
- Hickey W.J., Focht D.D. 1990. Degradation of mono-, di-, and trihalogenated benzoic acids by Pseudomonas aeruginosa JB2. Appl. Environ. Microbiol., v. 56, pp. 3842−3850.
- Hollender J., Hopp J., Dott W. 1997. Degradation of 4-chlorocatechol via the meta cleavage pathway by Comamonas testosteroni JH5. Appl. Environ. Microbiol., v. 63, pp. 4567−4572.
- Houghton J.E., Brown T.M., Appel A.J., Hughes E.J., Ornston L.N. 1995. Discontinuities in the evolution of Pseudomonas putida cat genes. J. Bacteriol., v. 177, pp. 401−412.
- Janke D., Ihn W. 1989. Cometabolic turnover of aniline phenol and some of their monochlorinated derivatives by the Rhodococcus mutant strain AM 144. Arch. Microbiol., v. 152, pp. 347−352.
- Kasberg Π’., Daubaras D.L., Chakrabarty A.M., Kinzelt D., Reineke W. 1995. Evidence that operons tcb, tfd, and clc encode maleylacetate reductase, the fourth enzyme of the modified ortho pathway. J. Bacteriol., v. 177, pp. 3885−3889.
- Kasberg Π’., Seibert V., Schlomann M., Reineke W. 1997. Cloning, characterization, and sequence analysis of the clcE gene encoding the maleylacetate reductase of Pseudomonas sp. strain B13. J. Bacteriol., v. 179, pp. 3801−3803.
- Kaschabek S., Reineke W. 1993. Degradation of chloroaromatics: purification and characterization of maleylacetate reductase from Pseudomonas sp. strain Π13. J. Bacteriol., v.175, pp. 6075−6081.
- Kaschabek S., Reineke W. 1995. Maleylacetate reductase of Pseudomonas sp. strain B13: specificity of substrate conversion and halide elimination. J. Bacteriol., v. 177, pp. 320−325.
- Katti S.K., Katz B.A., WyckofFH.W. 1989. Crystal structure of muconolactone isomerase at 3−3 A resolution. J. Mol. Biol., v. 205, pp. 557−571.
- Kaulmann U., Kaschabek SR., Schlomann M. 2001. Mechanism of chloride elimination from 3-chloro- and 2,4-dichloro-c7.v, 6vs-muconate: new insight obtained from analysis of muconate cycloisomerase variant CatB-K169A. J. Bacteriol., v. 183, pp. 4551−4561.
- Kilbane J, J. 1989. Desulfurization of coal: the microbial solution. Trends Biotechnol., v. 7, pp. 97−100.
- Kitunen V., Valo R., Salkinoja-Salonen M. 1987. Contamination of soil around wood-preserving facilities by polychlorinated aromatic compounds. Environ. Sci. Technol., v. 21, pp. 96−101.
- Π1Π΅Π±ΠΊΠ° G.M., Gibson D.T. 1981. Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol. Appl, Environ. Microbiol., v. 41, pp. 11 591 165.
- Krug M., Ziegler H., Straube G. 1985. Degradation of phenolic compounds by the yeast Candida tropicalis HP 15. J. Basic Microbiol., v. 25, pp. 103−110.
- Kuhm A.E., Schlfimann M., Knackmuss H.-J., Pieper D.H. 1990. Purification and characterization of dichloromuconate cycloisomerase from Alcaligenes eutrophus JMP 134. Biochem. J., v. 266, pp. 877−883.
- Kukor J.J., Olsen R.H., Siak J.-S. 1989. Recruitment of a chromosomally encoded maleylacetate reductase for degradation of 2,4-dichlorophenoxyacetic acid by plasmid pJP4. J. Bacteriol., v. 171, pp. 3385−3390.
- Laine M.M., Jorgensen K.S. 1996. Straw compost and bioremediated soil as inocula for the bioremediation of chlorophenol-contaminated soil. Appl. Environ. Microbiol., v. 62, pp. 1507−1513.
- Laemmly U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, v. 227, pp. 680−685.
- Larkin M.J., Mot R.D., Kulakov L.A., Nagy I. 1998. Applied aspects of Rhodococcus genetics. Antonie vanLeeuwenhoek, v. 74, pp. 133−153.
- Latorre J., Reinecke W., Knackmuss H.-J. 1984. Microbial metabolism of chloroanilines: enhanced evolution by natural genetic exchange. Arch. Microbiol., v. 140, pp. 159−165.
- Levy C.C. 1967, Melilotate hydroxylase. Purification of the enzyme and the nature of the prosthetic group. J. Biol. Chem., v. 242, pp. 747−753.
- Liu T.L., Chapman PJ. 1984. Purification and properties of a plasmid-encoded 2,4-dichlorophenol hydroxylase. FEBS Lett., v. 173, pp. 314−318.
- Mars A.E., Kasberg Π’., Kaschabek S.R., van Agteren M.H., Janssen D.B., Reineke W. 1997. Microbial degradation of chloroaromatics: use of the /we/a-cleavage pathway for mineralization of chlorobenzene. J.' Bacteriol., v. 179, pp. 4530−4537.
- Mathew C.D., Nagasawa Π’., Kobayashi M., Yamada H. 1988. Nitrilase-catalyzed production of nicotinic acid from 3-cyanopyridine in Rhodococcus rhodochrous Jl. Appl. Environ. Microbiol., v. 54, pp. 1030−1032.
- Mazur P., Pieken W.A., Budihas S.R., Williams S.E., Wong S" Kozarich J.W. 1994. C/.s.c/s-muconate lactonizing enzyme from Trichosporon cutaneum. evidence for a novel class of cycloisomerases in eucaryotes. Biochemistry, v. 33, pp. 1961−1970.
- Maltseva O.V., Solyanikova I.P., Golovleva L.A. 1994a. Chlorocatechol 1,2-dioxygenase from Rhodococcus opacus ICP. Kinetic and immunochemical comparison with analogous enzymes fron Gram-negative strains. Eur. J. Biochem., v. 226, pp. 1053−1061.
- Maltseva O.V., Solyanikova I.P., Golovleva L.A., Schlomann M., Knackmuss H.-J. 1994b. Dienlactone hydrolase from Rhodococcus opactis ICP: purification and properties. Arch. Microbiol., v. 162, pp. 368−374.
- MarchukD., Drumm M., Saulino A., Collins F.S. 1991. Construction of T-vectors, a rapid and general system for direct cloning of unmodified PCR products. Nucleic Acids Res., v. 19, p. 1154.
- Massey V. 1994. Activation of molecular oxygen by flavins and flavoproteins. J. Biol. Chem., v. 269, pp. 22 459−22 462.
- McGorkle G.M., Yeh W.-K., Fletcher P., Ornston L.N. 1980. Repetitions in the NH2-terminal amino acid sequence of /2-ketoadipate enol-lactone hydrolase from Pseudomonas putida. J. Biol. Chem., v. 255, pp. 6335−6341.
- McFall S.M., Chugani S.A., Chakrabarty A.M. 1998. Transcriptional activation of the catechol and chlorocatechol operons: variations on a theme. Gene, v. 223, pp. 257−267.
- McFall S.M., Parsek M.R., Chakrabarty A.M. 1997. 2-Chloromuconate and ClcR-mediated activation of the ck ABD operon: in vitro transcriptional and DNase I footprint analyses. J. Bacteriol., v. 179, pp. 3655−3663.
- Mohn W.W., Tiedje J.M. 1992. Microbial reductive dehalogenation. Microbiol. Rev., v. 56, pp. 482−507.i1
- Miiller C., Petruschka L., Cuypers H., Burchhardt G., Herrmann H. 1996. Carbon catabolite repression of phenol degradation in Pseudomonas putida is mediated by theinhibition of the activator protein PhlR. J. Bacterid., v. 178, pp. 2030−2036.
- Miiller D., Schl6mannM., Reineke W. 1996b. Maleylacetate reductases in chloroaromatic-degrading bacteria u^tng the modified ortho pathway: comparison of catalytic properties. J. Bacterid., v. 178, pp. 298−300.
- Murai N., Skoog F., Doyle M. E., Hanson R.S. 1980. Relationship between cytokinin production, presence of plasmids and fasciation caused by strains of Corynebacterium fascicms. Proc. Natl. Acad. Sci. USA, v. 77, pp. 619−623.
- Nagasawa Π’., Mathew C.D., Mauger J., Yamada H. 1988. Nitrile hydratase-catalyzed production of nicotinamide from 3-cyanopyridine in Rhodococcus rhodochrous Jl. Appl. Environ. Microbiol., v. 54, pp. 1766−1769.
- Nakai C., Hori K., Kagamiyama H., Nakazawa Π’., Nozaki M. 1983. Purification, subunit structure, and partial amino acid sequence of metapyrocatechase. J. Biol. Chem., v. 258, pp. 2916−2922.
- Nakai C., Horiike K., Kuramitsu S., Kagamiyama H., Nozaki M. 1990. Three isozymes of catechol 1,2-dioxygenase (pyrocatechase), aa, aP, PP, from Pseudomonas arvilla C-l. J. Biol. Chem., v. 265, pp. 660−665.
- Nakai C., Kagamiyama H., Saeki Y., Nozaki M. 1987. Nonidentical subunits of pyrocatechase from Pseudomonas arvilla C-l. Arch. Biochem. Biophys., v. 195, pp. 12−22.
- Nakai C., Nakazawa Π’., Nozaki M. 1988. Purification and properties of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla: C-1. Arch. Biochem. Biophys., v. 267, pp. 701−713.
- Neujahr H.Y., Varga J.M. 1970. Degradation of phenols by intact cells and cell-free preparations of Trichosporon cutaneum. Eur. J. Biochem., v. 13, pp. 37−44.
- Ngai K-L., Ornston L.N. 1988. Abundant expression of Pseudomonas genes for chlorocatechol metabolism. J. Bacterid., v. 170, pp. 2412−2413.
- Ngai K.-L., Schl6mann M., Knackmuss H.-J., Ornston L.N. 1987. Dienelactone hydrolase from Pseudomonas sp. strain B13. J. Bacteriol., v. 169, pp. 699−703.
- Nordlund I., Powlowski J., Shingler V. 1990. Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacterid., v. 172, pp. 6826−6833.
- Nurk A., Kasak L., Kivisaar M. 1991. Sequence of the gene (pheA) encoding phenol monooxygenase from Pseudomonas sp. EST 1001: expression in Escherichia coli and Pseudomonas putida. Gene, v. 102, pp. 13−18.
- Nurk A., Tamm Π., ΠΠ±Π³Π°ΠΊ R" Kivisaar M. 1993. In-vivo-generated fusion promoters in Pseudomonas putida. Gene, v. 127, pp. 23−29.
- OgawaN., McFall S.M., Klem T.J., Miyashita K., Chakrabarty A.M. 1999. Transcriptional activation of the chlorocatechol degradative genes of Ralstonia eutropha NH9. J. Bacteriol., v. 181, pp. 6697−6705.
- Ogawa N., Miyashita K. 1995. Recombination of a 3-chlorobenzoate catabolic plasmid from Alcaligenes eutrophus NH9 mediated by direct repeat elements. Appl. Environ. Microbiol., v. 61, ppj 3788−3795.
- Ohlendorf D.H., Lipscomb J.D., Weber P.C. 1988. Structure and assembly of protocatechuate 3,4-dioxygenase. Nature, v. 336, pp. 403−405.
- Ohlendorf D. FL, Ofville A.M., Lipscomb J.D. 1994. Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution. J. Mol. Biol., v. 244, pp. 586−608.
- Olsen R.H., Kukor J J., Kaphammer B. 1994. A novel toluene-3-monooxygenase pathway cloned from Pseudomonaspickettii PKO1. J. Bacteriol., v. 176, pp. 3749−3756.
- Omston L.N. 1966a. The conversion of catechol and protocatechuate to y9-ketoadipate by Pseudomonas putida. Π. Enzymes of the protocatechuate pathway. J. Biol. Chem., v. 241, pp. 3787−3794.
- Omston L.N. 1966b. The conversion of catechol and protocatechuate to /0-ketoadipate by Pseudomonas putida. III. Enzymes of the catechol pathway. J. Biol. Chem., v. 241, pp.3795−3799.
- Ornston L.N. 1966c. The conversion of catechol and protocatechuate to /?-ketoadipate by Pseudomonas putida. VI. Regulation. J. Biol. Chem., v. 241, pp. 3800−3810.
- Oxenford C.J., Ratcliffe R.C., Ramsay G.C. 1987. Rhodococcus equi infection in a cat.
- Aust. Vet. J., v. 64, p. 121. i
- Parsek M.R., Shinabarger D.L., Rothmel R.K., Chakrabarty A.M. 1992. Roles of CatR and c/s, c/'s-muconate in activation of the catBC operon, which is involved in benzoate degradation in Pseudomonas putida. J. Bacteriol., v. 174, pp. 7798−7806.
- Patel R.N., Meagher R.B., Ornston L.N. 1974. Relationships among enzymes of the P~ ketoadipate pathway: IV. Muconolactone isomerase from Acinetohacter calcoaceticus and Pseudomonas putida. J. Biol. Chem., v. 249, pp. 7410−7419.
- Pathak D., Ollis D. 1990. Refined structure of dienelactone hydrolase at 1−8 A. J. Mol. Biol., v. 214, pp. 497−525.
- Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F. 1990. Organization and sequence analysis of the 2,4-dichlorophenol hydrolase and dichlorocatechol oxidative operons of plasmid pJP4. J. Bacteriol., v. 172, pp. 2351−2359.
- Pieper D.H., Engesser K.-H., Don R.H., Timmis K.N., Knackmuss H.-J. 1985. Modified ortho-cleavage pathway in Alcaligenes eutrophus JMP134 for the degradation of 4-methylcatechol. FEMS Microbiol. Lett., v. 29, pp. 63−67.
- Pieper D.H., Reineke W., Engesser K.-H., Knackmuss H.-J 1988. Metabolism of 2,4-dichlorophenoxyacetic acid, 4-chloro-2-methylphenoxyacetic acid and 2-methylphenoxyacetic acid by Alcaligenes eutrophus JMP 134. Arch. Microbiol., v. 150, pp. 95−102.
- Powlowski J.B., Dagley S. 1985. /Mcetoadipate pathway in Trichosporon cutaneum modified for methyl-substituted metabolites. J. Bacteriol., v. 163, pp. 1126−1135.
- Powlowski J.B., Shingler V. 1990. In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacteriol., v. 172, pp. 6834−6840.
- Prescott J.F. 1991. Rhodococcus equi: an animal and human pathogen. Clin. Microbiol. Rev., v. 4, pp. 20−34.
- Prucha M., Peterseim A., Timmis K.N., Pieper D.H. 1996a. Muconolactone isomerase of the 3-oxoadipate pathway catalyzes dechlorination of. 5-chloro-substituted muconolactones. Eur. J. Biochem., v. 237, pp. 350−356.
- Prucha M., Wray V., Pieper D.H. 1996b. Metabolism of 5-chlorosubstituted muconolactones. Eur. J. Biochem., v. 237, pp. 357−366.
- Prucha M., Peterseim A., Pieper D.H. 1997. Evidence for an isomeric muconolactone isomerase involved in the metabolism of 4-methylmuconolactone by Alcaligenes eutrophus JMP 134. Arch. Microbiol., v. 168, pp. 33−38.
- Qian H., Edlund Xjj- Powlowski J.B., Shingler V., Sethson. 1997. Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy. Biochemistry, v. 36, pp. 495−504.
- Rast H.G., Engelhardt G., Wallnofer P.R. 1980. Degradation of aromatic compounds in the actinomycete-genus Rhodococcus. FEMS Microbiol. Lett., v. 7, pp. 1−6.
- Reineke W., Knackmuss H.-J. 1980. Hybrid pathway for chlorobenzoate metabolism in Pseudomonas sp. Π13 derivatives. J. Biol. Chem., v. 142, pp. 467−473.
- Riegert U., Heiss G., Fischer P., Stolz A. 1998. Distal cleavage of 3-chlorocatechol by an extradiol dioxygenase to 3-chloro-2-hydroxymuconic semialdehyde. J. Bacteriol., v. 180, pp. 2849−2853.
- Romero-Arroyo C.E., Schell M.A., Gaines G.L.I., Neidle E L. 1995. catM encodes a LysR-type transcriptional activator regulating catechol degradation in Acinetobacter calcoaceticus. J. Bacteriol., v. 177, pp. 5891−5898.
- Sallis P.J., Armfield S.J., Bull A.T., Hardman D.J. 1990. Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2. J. Gen. Microbiol., v. 136, pp. 115−120.
- Sambrook J., Fritsch E.F., Maniatis T. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N Y.
- Schell M.A. 1993. Molecular biology of the LysR family of transcriptional regulators. Ann. Rev. Microbiol., v. 47, pp. 597−626.
- Schtomann M., Ngai K.-L., Ornston L.N., Knackmuss H.-J. 1993. Dienelactone hydrolase from Pseudomonas cepacia. J. Bacteriol., v. 175, pp. 2994−3001.
- Schlomann Π., Schmidt Π., Knackmuss H.-J. 1990a. Different types of dienelactonehydrolase in 4-fluorobenzoate-utilizing bacteria. J. Bacteriol., v. 172, pp. 5112−5118.u
- Schmidt E. 1987. Response of a chlorophenols degrading mixed culture to changing loads of phenol, chlorophenol and cresols. Appl. Microbiol. Biotechnol., v. 27, pp. 94−99.
- Schmidt E., Knackmuss H.-J. 1984. Production of cis, cis-muconate from benzoate and 2-fluoro-c/Xm-muconate from 3-fluorobenzoate by 3-chlorobenzoate degrading bacteria. Appl. Microbiol. Biotechnol., v. 20, pp. 351−355.
- Schmidt E., Knackmuss H.-J. 1980. Chemical structure and biodegradability of halogenated aromatic compound: conversion of chlorinated muconic acids into maleoylacetic acid. Biochem. J., v. 192, pp. 339−347.
- Schukat Π., Janke D., Krebs D., Fritsche W. 1983. Cometabolic degradation of 2- and 3-chloroaniline because of glucose metabolism by Rhodococcus sp. An 117. Curr. Microbiol, v. 9, pp. 81−86.
- Seibert V., Kourbatova E.M., Golovleva L.A., Schlomann M. 1998. Characterization of the maleylacetate reductase MacA of Rhodococcus opacus ICP and evidence for the presence of an isofunctional enzyme. J. Bacteriol, v. 180, pp. 3503−3508.
- Seibert V., Stadler-Fritzsche K., Schlftmann M. 1993. Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134 (pJP4). J. Bacteriol, v. 175, pp. 6745−6754.
- Sejlitz Y., Neujahr H.Y. 1987. Phenol hydroxylase from yeast. A model for phenol binding and an improved purification procedure. Eur. J. Biochem., v. 170, pp. 343−349.
- Sistrom W.R., Stanier R.Y. 1954. The mechanism of formation of /?-ketoadipic acid by bacteria. J. Biol. Chem., v. 210, pp. 821−836.
- Smith M.R. 1990, The biodegradation of aromatic hydrocarbons by bacteria. Biodegradation, v. 1, pp. 191−206.
- Straube G. 1990. Phenol hydroxylase from Rhodococcus sp. PI. J. Basic Microbiol., v. 27, pp. 229−232.
- Straube G., Hensel J4 Niedan C., Straube E. 1990. Kinetic studies of phenol degradation by Rhodococcus sp. PI. I. Batch cultivation. Antonie van Leeuwenhoek J. Microbiol. Ser., v. 57, pp. 29−32.
- Strickland S., Massey V. 1973a. The purification and properties of the flavoprotein melilotate hydroxylase. J. Biol. Chem., v. 248, pp. 2944−2952.
- Strickland S., Massey V. 1973b. The mechanism of action of the flavoprotein melilotate hydroxylase. J. Biol. Chem., v. 248, pp. 2953−2962.
- Sugimoto K., Senda Π’., Aoshima H., Masai E., Fukuda M., Mitsui Y. 1999. Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions. Structure, v. 7, pp. 953−965.
- Suske W.A., van Berkel W.J.H., Kohler H.-P. E. 1999. Catalytic mechanism of 2-hydroxybiphenyl 3-rnonooxygenase, a flavoprotein from Pseudomonas azelaica HBP1. J. Biol. Chem., v. 274, pp. 33 355−33 365.i
- Sylvestre M., Mailhiot K., Ahmad D., Masse R. 1989. Isolation and preliminary characterization of a 2-chlorobenzoate degrading Pseudomonas. Can. J. Microbiol., v. 35, pp. 439−443.
- Vetting M.W., Ohlendorf D.H. 2000. The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. Structure, v. 8, pp. 429−440.
- Vollmer M.D., Schlomann M. 1995. Conversion of 2-chloro-c'", c/.y-muconate and its metabolites 2-chlord- and 5-chloromuconoIactone by chloromuconate cycloisomerases of pJP4 and pAC27. J iBacteriol., v. 177, pp. 2938−2941.
- Vollmer M.D., Fischer P., Knackmuss H.-J., Schlomann M. 1994. Inability of muconate cycloisomerases to cause dehalogenation during conversion of 2-chloro-67.v, 67. v-muconate. J. Bacteriol., v. 176 pp. 4366−4375.
- Wallis M.G., Chapshan K. 1990. Isolation and partial characterization of an extradiol non-haem iron dioxygenase which preferentially cleaves 3-methylcatechol. Biochem. J., v. 266, pp. 605−609.
- Wang L., Helmann J.D., Winans S.C. 1992. The A. tumefaciens transcriptional activator Occll causes a bend at a target promoter, which is partially relaxed by a plant tumor metabolite. Cell, v. 69, pp. 659−667.
- Warhurst A.M., Fewson C.A. 1994. Biotransformations catalyzed by the genus Rhodococcus. Critical Reviews in Biotechnology, v. 14, pp. 29−73.
- White-Stevens R.H., Kamin H. 1972a. Studies of a flavoprotein, salicylate hydroxylase. I. Preparation, properties, and the uncoupling of oxygen reduction from hydroxylation. J. Biol. Chem., v. 247, pp. 2358−2370.
- White-Stevens R.H., Kamin H. 1972b. Studies of a flavoprotein, salicylate hydroxylase. II. Enzyme mechanism. J. Biol. Chem., v. 247, pp. 2371−2381.
- Whittaker J.W., Lipscomb J.D., Kent T.A., Munck E. 1984. Brevibactehum fuscum protocatechuate 3,4-dioxygenase: purification, crystallization, and characterization. J. Biol. Chem., v. 259, pp. 4466−4475.
- Wieser M., Eberspacher J., Vogler Π., Lingens F. 1994. Metabolism of 4-chlorophenol by Azotobacter sp. strain GP1: structure of the meta cleavage product of 4-chIorocatechol. FEMS Microbiol., Lett., v. 116, pp. 73−78.
- Williams P.A., Murray K. 1974. Metabolism of benzoate and the methylbenzoates by Pseudomonas putida {arvilla) mt-2: evidence for the existence of a TOL plasmid. J. Bacteriol., v. 120, pp. 416−423.
- Winkler J., Eltis L.D., Dwyer D.F., Rohde M. 1995. Tetrameric structure and cellular location of catechol 2,3-dioxygenase. Arch. Microbiol., v. 163, pp. 65−69.
- Yeh W.-K., Fletcher P., Ornston L.N. 1980. Homologies in the NH2-terminal amino acid sequence of y-carboxymuconolactone decarboxylases and muconolactone isomerases. J. Biol. Chem., v. 255, pp. 6347−6354.
- Yeh W.-K., Ornston L.N. 1984. /^-Chloromercuribenzoate specifically modifies thiols associated with the active sites of/i-ketoadipate enol-lactone hydrolase and succinyl Co A. /?-ketoadipate CoA transferase. Arch Microbiol, v. 138, pp. 102−105.
- Zaitsev G.M., Uotila J.S., Tsitko I.V., Lobanok A.G., Salkinoja-Salonen M.S. 1995. Utilization of halogenated benzenes, phenols, and benzoates by Rhodococcus opacus GM-14. Appl. Environ. JViicrobiol., v. 61, pp. 4191−4201.