ΠΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ β ?-Π»ΠΈΠ°Π·Π° Citrobacter freundii: ΠΎΡΠΈΡΡΠΊΠ°, ΠΊΡΠΈΡΡΠ°Π»Π»ΠΈΠ·Π°ΡΠΈΡ, ΡΠΈΠ·ΠΈΠΊΠΎ-Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΈ ΠΊΠ°ΡΠ°Π»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΡ ΠΏΡΠΈΡΠΎΠ΄Π½ΠΎΠ³ΠΎ ΠΈ ΡΠ΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΠΎΠ³ΠΎ ΡΠΈΠΏΠΎΠ²
Π ΠΏΠΎΡΠ»Π΅Π΄Π½Π΅Π΅ Π΄Π΅ΡΡΡΠΈΠ»Π΅ΡΠΈΠ΅, Π² ΠΎΡΠ½ΠΎΠ²Π½ΠΎΠΌ Π±Π»Π°Π³ΠΎΠ΄Π°ΡΡ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠ² ΡΠ΅Π½ΡΠ³Π΅Π½ΠΎΡΡΡΡΠΊΡΡΡΠ½ΠΎΠ³ΠΎ Π°Π½Π°Π»ΠΈΠ·Π° ΠΈ Π±ΡΡΡΡΠΎΠΉ ΠΊΠΈΠ½Π΅ΡΠΈΠΊΠΈ, ΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½Ρ Π΄Π΅ΡΠ°Π»ΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΈ ΠΏΡΠΎΡΡΡΠ°Π½ΡΡΠ²Π΅Π½Π½ΡΠ΅ ΡΡΡΡΠΊΡΡΡΡ Π΄Π»Ρ ΠΌΠ½ΠΎΠ³ΠΈΡ ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Ρ-5'-ΡΠΎΡΡΠ°Ρ-Π·Π°Π²ΠΈΡΠΈΠΌΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ², Π² ΠΏΠ΅ΡΠ²ΡΡ ΠΎΡΠ΅ΡΠ΅Π΄Ρ ΠΏΡΠΈΠ½Π°Π΄Π»Π΅ΠΆΠ°ΡΠΈΡ ΠΊ ΠΊΠ»Π°ΡΡΡ ΡΡΠ°Π½ΡΡΠ΅ΡΠ°Π·. ΠΠ½Π°ΡΠΈΡΠ΅Π»ΡΠ½ΡΠ΅ ΡΡΠΏΠ΅Ρ ΠΈ Π΄ΠΎΡΡΠΈΠ³Π½ΡΡΡ ΠΈ Π² ΡΡΡΡΠΊΡΡΡΠ½ΡΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡΡ . ΠΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΡΡΡΡΠΊΡΡΡΡ ΠΈ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠ° Π΄Π΅ΠΉΡΡΠ²ΠΈΡ… 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 ΠΎΠ±ΠΎΠ·Π½Π°ΡΠ΅Π½ΠΈΠΉ ΠΈ ΡΠΎΠΊΡΠ°ΡΠ΅Π½ΠΈΠΉ
ΠΠ±Π·ΠΎΡ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ. ΠΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Π°. ΠΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅ΠΌΡΡ ΡΠ΅Π°ΠΊΡΠΈΠΉ, ΡΡΡΡΠΊΡΡΡΠ° ΠΈ ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ Π² ΠΌΠ΅Π΄ΠΈΡΠΈΠ½Π΅.
1. Π₯ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΎΡΠ½ΠΎΠ²Ρ ΠΌΠ½ΠΎΠ³ΠΎΠΎΠ±ΡΠ°Π·ΠΈΡ ΡΠ΅Π°ΠΊΡΠΈΠΉ, ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅ΠΌΡΡ ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Ρ-5'-ΡΠΎΡΡΠ°Ρ Π·Π°Π²ΠΈΡΠΈΠΌΡΠΌΠΈ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΠΌΠΈ.:.Π³.
2. ΠΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Π°: ΡΠ΅Π°ΠΊΡΠΈΠΎΠ½Π½Π°Ρ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ½ΠΎΡΡΡ ΠΈ ΠΌΠ½ΠΎΠ³ΠΎΠΎΠ±ΡΠ°Π·ΠΈΠ΅ ΠΈΡΡΠΎΡΠ½ΠΈΠΊΠΎΠ².
3: ΠΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ ΡΠ΅Π°ΠΊΡΠΈΠΉ Π°, Ρ-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΈ Ρ-Π·Π°ΠΌΠ΅Π³ΡΠ΅Π½ΠΈΡ, ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅ΠΌΡΡ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ -Ρ-Π»ΠΈΠ°Π·ΠΎΠΉ ΠΈ Π΄ΡΡΠ³ΠΈΠΌΠΈ ΠΠΠ€-Π·Π°Π²ΠΈΡΠΈΠΌΡΠΌΠΈ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΠΌΠΈ, ΠΏΡΠΈΠ½Π°Π΄Π»Π΅ΠΆΠ°ΡΠΈΠΌΠΈ ΠΊ Ρ-ΡΠ΅ΠΌΠ΅ΠΉΡΡΠ²Ρ. «
4. ΠΡΠΈΡΡΠ°Π»Π»ΠΈΡΠ΅ΡΠΊΠ°Ρ ΡΡΡΡΠΊΡΡΡΠ° ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ.
5. ΠΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ Π² ΠΌΠ΅Π΄ΠΈΡΠΈΠ½Π΅.
ΠΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ β ?-Π»ΠΈΠ°Π·Π° Citrobacter freundii: ΠΎΡΠΈΡΡΠΊΠ°, ΠΊΡΠΈΡΡΠ°Π»Π»ΠΈΠ·Π°ΡΠΈΡ, ΡΠΈΠ·ΠΈΠΊΠΎ-Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΈ ΠΊΠ°ΡΠ°Π»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΡ ΠΏΡΠΈΡΠΎΠ΄Π½ΠΎΠ³ΠΎ ΠΈ ΡΠ΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΠΎΠ³ΠΎ ΡΠΈΠΏΠΎΠ² (ΡΠ΅ΡΠ΅ΡΠ°Ρ, ΠΊΡΡΡΠΎΠ²Π°Ρ, Π΄ΠΈΠΏΠ»ΠΎΠΌ, ΠΊΠΎΠ½ΡΡΠΎΠ»ΡΠ½Π°Ρ)
Π€Π΅ΡΠΌΠ΅Π½ΡΡ, ΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΠ΅ Π² ΠΊΠ°ΡΠ΅ΡΡΠ²Π΅ ΠΊΠΎΡΠ°ΠΊΡΠΎΡΠ° ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Ρ-5'-ΡΠΎΡΡΠ°Ρ, ΠΈΠ³ΡΠ°ΡΡ ΠΏΠ΅ΡΠ²ΠΎΡΡΠ΅ΠΏΠ΅Π½Π½ΡΡ ΡΠΎΠ»Ρ Π² Π°Π·ΠΎΡΠΈΡΡΠΎΠΌ ΠΎΠ±ΠΌΠ΅Π½Π΅. ΠΠ½ΠΈ ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΡΡ ΡΠ°Π·Π½ΠΎΠΎΠ±ΡΠ°Π·Π½ΡΠ΅ ΡΠ΅Π°ΠΊΡΠΈΠΈ ΠΏΡΠ΅Π²ΡΠ°ΡΠ΅Π½ΠΈΠΉ Π°ΠΌΠΈΠ½ΠΎΠΊΠΈΡΠ»ΠΎΡΡΡΠ°Π½ΡΠ°ΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅, ΡΠ°ΡΠ΅ΠΌΠΈΠ·Π°ΡΠΈΡ, Π°ΠΈ Π -Π΄Π΅ΠΊΠ°ΡΠ±ΠΎΠΊΡΠΈΠ»ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅, ΡΠ΅ΡΡΠΎ-Π°Π»ΡΠ΄ΠΎΠ»ΡΠ½ΠΎΠ΅ ΡΠ°ΡΡΠ΅ΠΏΠ»Π΅Π½ΠΈΠ΅, (3- ΠΈ Ρ-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΈ Π·Π°ΠΌΠ΅ΡΠ΅Π½ΠΈΠ΅. Π¦Π΅Π½ΡΡΠ°Π»ΡΠ½Π°Ρ ΡΠΎΠ»Ρ ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Ρ-5'-ΡΠΎΡΡΠ°Ρ-Π·Π°Π²ΠΈΡΠΈΠΌΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ² Π² ΠΌΠ΅ΡΠ°Π±ΠΎΠ»ΠΈΠ·ΠΌΠ΅ Π°ΠΌΠΈΠ½ΠΎΠΊΠΈΡΠ»ΠΎΡ ΠΈ Π°ΠΌΠΈΠ½ΠΎΠ² ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΠ΅Ρ Π°ΠΊΡΡΠ°Π»ΡΠ½ΠΎΡΡΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠΎΠ² ΠΈΡ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΈ ΡΠ΅Π³ΡΠ»ΡΡΠΈΠΈ ΠΈΡ Π³Π΅Π½ΠΎΠ².
ΠΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Π° (ΠΠ€ 4.4.1.11) ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Ρ-5'-ΡΠΎΡΡΠ°Ρ-Π·Π°Π²ΠΈΡΠΈΠΌΡΠΉ ΡΠ΅ΡΠΌΠ΅Π½Ρ, ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΡΡΠΈΠΉ ΡΠ΅Π°ΠΊΡΠΈΡ Π°, Ρ-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ L-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½Π° (ΠΈΠ»ΠΈ Π΅Π³ΠΎ ΠΏΡΠΎΠΈΠ·Π²ΠΎΠ΄Π½ΡΡ ) Ρ ΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ Π°-ΠΊΠ΅ΡΠΎΠ±ΡΡΠΈΡΠ°ΡΠ°, ΠΌΠ΅ΡΠ°Π½ΡΠΈΠΎΠ»Π° ΠΈ Π°ΠΌΠΌΠΈΠ°ΠΊΠ°: ΠΎ ΠΎ.
Π€Π΅ΡΠΌΠ΅Π½Ρ ΡΠ°ΠΊΠΆΠ΅ ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅Ρ ΡΠ΅Π°ΠΊΡΠΈΡ Ρ-Π·Π°ΠΌΠ΅ΡΠ΅Π½ΠΈΡ L-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½Π° ΠΈ Π΅Π³ΠΎ Π°Π½Π°Π»ΠΎΠ³ΠΎΠ², Π° ΡΠ°ΠΊΠΆΠ΅ ΡΠ΅Π°ΠΊΡΠΈΠΈ Π°,|3-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΈ Ρ-Π·Π°ΠΌΠ΅ΡΠ΅Π½ΠΈΡ L-ΡΠΈΡΡΠ΅ΠΈΠ½Π° ΠΈ Π΅Π³ΠΎ Π°Π½Π°Π»ΠΎΠ³ΠΎΠ².
Π ΠΏΠΎΡΠ»Π΅Π΄Π½Π΅Π΅ Π΄Π΅ΡΡΡΠΈΠ»Π΅ΡΠΈΠ΅, Π² ΠΎΡΠ½ΠΎΠ²Π½ΠΎΠΌ Π±Π»Π°Π³ΠΎΠ΄Π°ΡΡ ΡΠ°Π·Π²ΠΈΡΠΈΡ ΠΌΠ΅ΡΠΎΠ΄ΠΎΠ² ΡΠ΅Π½ΡΠ³Π΅Π½ΠΎΡΡΡΡΠΊΡΡΡΠ½ΠΎΠ³ΠΎ Π°Π½Π°Π»ΠΈΠ·Π° ΠΈ Π±ΡΡΡΡΠΎΠΉ ΠΊΠΈΠ½Π΅ΡΠΈΠΊΠΈ, ΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½Ρ Π΄Π΅ΡΠ°Π»ΡΠ½ΡΠ΅ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΡ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΈ ΠΏΡΠΎΡΡΡΠ°Π½ΡΡΠ²Π΅Π½Π½ΡΠ΅ ΡΡΡΡΠΊΡΡΡΡ Π΄Π»Ρ ΠΌΠ½ΠΎΠ³ΠΈΡ ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Ρ-5'-ΡΠΎΡΡΠ°Ρ-Π·Π°Π²ΠΈΡΠΈΠΌΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ², Π² ΠΏΠ΅ΡΠ²ΡΡ ΠΎΡΠ΅ΡΠ΅Π΄Ρ ΠΏΡΠΈΠ½Π°Π΄Π»Π΅ΠΆΠ°ΡΠΈΡ ΠΊ ΠΊΠ»Π°ΡΡΡ ΡΡΠ°Π½ΡΡΠ΅ΡΠ°Π·. ΠΠ½Π°ΡΠΈΡΠ΅Π»ΡΠ½ΡΠ΅ ΡΡΠΏΠ΅Ρ ΠΈ Π΄ΠΎΡΡΠΈΠ³Π½ΡΡΡ ΠΈ Π² ΡΡΡΡΠΊΡΡΡΠ½ΡΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡΡ .
3-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΡΡΡΠΈΡ ΠΈ Π -Π·Π°ΠΌΠ΅ΡΠ°ΡΡΠΈΡ Π»ΠΈΠ°Π·. ΠΠ΄Π½Π°ΠΊΠΎ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Ρ-5'-ΡΠΎΡΡΠ°Ρ-Π·Π°Π²ΠΈΡΠΈΠΌΠΎΠΉ ΡΠ΅Π°ΠΊΡΠΈΠΈ Ρ-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ Π°ΠΌΠΈΠ½ΠΎΠΊΠΈΡΠ»ΠΎΡ ΡΠ²Π»ΡΠ΅ΡΡΡ ΠΎΠ΄Π½ΠΈΠΌ ΠΈΠ· Π½Π°ΠΈΠΌΠ΅Π½Π΅Π΅ ΠΈΠ·ΡΡΠ΅Π½Π½ΡΡ .
ΠΠ·ΡΡΠ΅Π½ΠΈΠ΅ ΡΡΡΡΠΊΡΡΡΡ ΠΈ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠ° Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΡ ΠΏΠΎΠ»ΡΡΠΈΡΡ Π½ΠΎΠ²ΡΠ΅ Π²Π°ΠΆΠ½ΡΠ΅ Π΄Π°Π½Π½ΡΠ΅ ΠΎ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌΠ΅ ΡΠ΅Π°ΠΊΡΠΈΠΈ Ρ-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΈ. Π·Π°ΠΊΠΎΠ½ΠΎΠΌΠ΅ΡΠ½ΠΎΡΡΡΡ Π²Π·Π°ΠΈΠΌΠΎΠΎΡΠ½ΠΎΡΠ΅Π½ΠΈΡ ΡΡΡΡΠΊΡΡΡΠ°-ΡΡΠ½ΠΊΡΠΈΡ, ΠΎΠ±Π΅ΡΠΏΠ΅ΡΠΈΠ²Π°ΡΡΠΈΡ ΡΠΏΠ΅ΡΠΈΡΠΈΡΠ½ΠΎΡΡΡ ΠΈ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΡΠ°Π·Π½ΠΎΠΎΠ±ΡΠ°Π·Π½ΡΡ ΠΏΡΠ΅Π²ΡΠ°ΡΠ΅Π½ΠΈΠΉ Π°ΠΌΠΈΠ½ΠΎΠΊΠΈΡΠ»ΠΎΡ ΠΏΡΠΈ ΡΡΠ°ΡΡΠΈΠΈ ΠΎΠ΄Π½ΠΎΠ³ΠΎ ΠΊΠΎΡΠ°ΠΊΡΠΎΡΠ°.
Π Π½Π°ΡΡΠΎΡΡΠ΅ΠΌΡ Π²ΡΠ΅ΠΌΠ΅Π½ΠΈ Π³Π΅Π½, ΠΊΠΎΠ΄ΠΈΡΡΡΡΠΈΠΉ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ, Π±ΡΠ» Π½Π°ΠΉΠ΄Π΅Π½ Π² Π±ΠΎΠ»ΡΡΠΎΠΌ ΠΊΠΎΠ»ΠΈΡΠ΅ΡΡΠ²Π΅ ΡΠ΅ΠΊΠ²Π΅Π½ΠΈΡΠΎΠ²Π°Π½Π½ΡΡ Π³Π΅Π½ΠΎΠΌΠΎΠ² ΠΌΠΈΠΊΡΠΎΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠΎΠ², Π² ΡΠΎΠΌ ΡΠΈΡΠ»Π΅ ΠΈ Π² Π½Π΅ΠΊΠΎΡΠΎΡΡΡ ΠΏΠ°ΡΠΎΠ³Π΅Π½Π½ΡΡ . Π€Π΅ΡΠΌΠ΅Π½Ρ Π±ΡΠ» ΡΠ°ΠΊΠΆΠ΅ Π½Π°ΠΉΠ΄Π΅Π½ Π² ΠΏΠ°ΡΠΎΠ³Π΅Π½Π½ΡΡ ΡΡΠΊΠ°ΡΠΈΠΎΡΠ°Ρ Trichomonas vaginalis ΠΈ Entamoeba hystolytica. ΠΠ΄Π½Π°ΠΊΠΎ ΡΡΠΎΡ Π³Π΅Π½ Π½Π΅ Π½Π°ΠΉΠ΄Π΅Π½ Ρ ΠΌΠ»Π΅ΠΊΠΎΠΏΠΈΡΠ°ΡΡΠΈΡ . ΠΠΎΡΡΠΎΠΌΡ ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΡΡ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ ΠΌΠΎΠ³ΡΡ Π±ΡΡΡ Π½ΠΎΠ²ΡΠΌΠΈ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΡΠΌΠΈ Π°Π½ΡΠΈΠΏΠ°ΡΠΎΠ³Π΅Π½Π½ΡΠΌΠΈ ΡΡΠ΅Π΄ΡΡΠ²Π°ΠΌΠΈ.
Π 70-Ρ Π³ΠΎΠ΄Π°Ρ ΡΡΠ°Π»Π° ΠΈΠ·Π²Π΅ΡΡΠ½Π° Π°Π±ΡΠΎΠ»ΡΡΠ½Π°Ρ ΠΏΠΎΡΡΠ΅Π±Π½ΠΎΡΡΡ ΠΌΠ½ΠΎΠ³ΠΈΡ ΡΠ°ΠΊΠΎΠ²ΡΡ ΠΊΠ»Π΅ΡΠΎΠΊ Π² ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½Π΅ ΠΈ Π² ΠΏΠΎΡΠ»Π΅Π΄Π½Π΅Π΅ Π²ΡΠ΅ΠΌΡ ΠΏΠΎΡΠ²Π»ΡΠ΅ΡΡΡ Π²ΡΠ΅ Π±ΠΎΠ»ΡΡΠ΅ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠΉ, ΡΠ²ΡΠ·Π°Π½Π½ΡΡ Ρ ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ΠΌ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ ΠΊΠ°ΠΊ ΠΏΡΠΎΡΠΈΠ²ΠΎΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΠΎΠ³ΠΎ Π°Π³Π΅Π½ΡΠ°. ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Π²Π²Π΅Π΄Π΅Π½ΠΈΠ΅ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ (ΠΊΠ°ΠΊ Π±Π΅Π»ΠΊΠΎΠ²ΠΎΠ³ΠΎ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠ°, ΡΠ°ΠΊ ΠΈ Π² ΡΠΎΡΡΠ°Π²Π΅ ΡΠ΅ΡΡΠΎΠΈ Π°Π΄Π΅Π½ΠΎΠ²ΠΈΡΡΡΠ½ΠΎΠ³ΠΎ Π²Π΅ΠΊΡΠΎΡΠΎΠ²) Π² ΠΎΠΏΡΡ ΠΎΠ»Π΅Π²ΡΠ΅ ΠΊΠ»Π΅ΡΠΊΠΈ ΠΏΡΠΈΠ²ΠΎΠ΄ΠΈΡ ΠΊ ΠΈΡ Π³ΠΈΠ±Π΅Π»ΠΈ. Π ΡΠ°ΠΊΠΎΠ²ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ Π² ΠΏΡΠΈΡΡΡΡΡΠ²ΠΈΠΈ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ Π½Π°Π±Π»ΡΠ΄Π°Π»ΠΎΡΡ Π·Π½Π°ΡΠΈΡΠ΅Π»ΡΠ½ΠΎΠ΅ ΡΠ½ΠΈΠΆΠ΅Π½ΠΈΠ΅ ΡΡΠΎΠ²Π½Ρ ΠΌΠ΅ΡΠΈΠ»ΠΈΡΠΎΠ²Π°Π½Π½ΠΎΠΉ Π³Π΅Π½ΠΎΠΌΠ½ΠΎΠΉ ΠΠΠ, ΠΊΠΎΡΡΠ΅Π»ΠΈΡΠΎΠ²Π°Π²ΡΠ΅Π΅ Ρ Π·Π°ΠΌΠ΅Π΄Π»Π΅Π½ΠΈΠ΅ΠΌ ΡΠΎΡΡΠ° ΠΊΠ»Π΅ΡΠΎΠΊ.
ΠΠΏΠ΅ΡΠ²ΡΠ΅ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Π° Π±ΡΠ»Π° ΠΏΠΎΠ»ΡΡΠ΅Π½Π° Π² Π³ΠΎΠΌΠΎΠ³Π΅Π½Π½ΠΎΠΌ Π²ΠΈΠ΄Π΅ ΡΡΠ°Π²Π½ΠΈΡΠ΅Π»ΡΠ½ΠΎ Π½Π΅Π΄Π°Π²Π½ΠΎ — Π² 1977 Π³. ΠΈΠ· ΠΊΠ»Π΅ΡΠΎΠΊ Pseudomonas putida. Π Π½Π°ΡΡΠΎΡΡΠ΅ΠΌΡ Π²ΡΠ΅ΠΌΠ΅Π½ΠΈ ΠΎΡΠΈΡΠ΅Π½Π° ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Π° Π½Π΅ΡΠΊΠΎΠ»ΡΠΊΠΈΡ ΠΈΡΡΠΎΡΠ½ΠΈΠΊΠΎΠ² (Pseudomonas putida, Pseudomonas ovalis, Aeromonas, Brevibacterium lines, Trichomonas vaginalis, Pseudomonas taetrolens ΠΈ Citrobacter freundii), ΠΎΠ΄Π½Π°ΠΊΠΎ Π΄Π°Π½Π½ΡΠ΅ ΠΎ ΡΠΈΠ·ΠΈΠΊΠΎ-Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΡ ΠΈ ΠΊΠ°ΡΠ°Π»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΡ ΡΠ²ΠΎΠΉΡΡΠ²Π°Ρ ΡΡΠΈΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ² Π²Π΅ΡΡΠΌΠ° ΠΎΠ³ΡΠ°Π½ΠΈΡΠ΅Π½Ρ.
Π ΡΠ²ΡΠ·ΠΈ Ρ ΠΏΠ΅ΡΡΠΏΠ΅ΠΊΡΠΈΠ²Π½ΠΎΡΡΡΡ ΠΈΡΠΏΠΎΠ»ΡΠ·ΠΎΠ²Π°Π½ΠΈΡ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ Π² ΠΌΠ΅Π΄ΠΈΡΠΈΠ½Π΅ ΡΠ΅Π»Π΅ΡΠΎΠΎΠ±ΡΠ°Π·Π½ΠΎ Π²ΡΠ΅ΡΡΠΎΡΠΎΠ½Π½Π΅ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°ΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΡ, Π²ΡΠ΄Π΅Π»Π΅Π½Π½ΡΠ΅ ΠΈΠ· ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΠΈΡΡΠΎΡΠ½ΠΈΠΊΠΎΠ².
Π¦Π΅Π»ΡΡ Π΄Π°Π½Π½ΠΎΠΉ ΡΠ°Π±ΠΎΡΡ ΡΠ²Π»ΡΠ»ΠΎΡΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ ΡΠΈΠ·ΠΈΠΊΠΎ-Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΡ ΠΈ ΠΊΠ°ΡΠ°Π»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΠΎΠ² ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ Citrobacter freundii.
Π ΡΠ°Π±ΠΎΡΠ΅ Π±ΡΠ»ΠΈ ΠΏΠΎΡΡΠ°Π²Π»Π΅Π½Ρ ΡΠ»Π΅Π΄ΡΡΡΠΈΠ΅ Π·Π°Π΄Π°ΡΠΈ:
1)ΡΠ°Π·ΡΠ°Π±ΠΎΡΠΊΠ° ΠΌΠ΅ΡΠΎΠ΄Π° ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΡ Π³ΠΎΠΌΠΎΠ³Π΅Π½Π½ΠΎΠ³ΠΎ ΠΏΡΠ΅ΠΏΠ°ΡΠ°ΡΠ° ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ Citrobacter freundii,.
2) ΠΊΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΈ ΡΠ΅ΠΊΠ²Π΅Π½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ Π³Π΅Π½Π° ΡΠ΅ΡΠΌΠ΅Π½ΡΠ° ΠΈ ΡΠΎΠ·Π΄Π°Π½ΠΈΠ΅ ΡΡΠ°ΠΌΠΌΠ°-ΡΡΠΏΠ΅ΡΠΏΡΠΎΠ΄ΡΡΠ΅Π½ΡΠ°,.
3) ΠΎΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΡΡΠ°ΡΠΈΠΎΠ½Π°ΡΠ½ΡΡ ΠΊΠ°ΡΠ°Π»ΠΈΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΠΎΠ² ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°,.
4) ΠΏΠΎΠΈΡΠΊ ΡΡΠ»ΠΎΠ²ΠΈΠΉ Π²ΡΡΠ°ΡΠΈΠ²Π°Π½ΠΈΡ ΠΊΡΠΈΡΡΠ°Π»Π»ΠΎΠ² ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ, ΠΏΡΠΈΠ³ΠΎΠ΄Π½ΡΡ Π΄Π»Ρ ΡΠ΅Π½ΡΠ³Π΅Π½ΠΎΡΡΡΡΠΊΡΡΡΠ½ΡΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠΉ.
Π‘ΠΏΠΈΡΠΎΠΊ ΠΎΠ±ΠΎΠ·Π½Π°ΡΠ΅Π½ΠΈΠΉ ΠΈ ΡΠΎΠΊΡΠ°ΡΠ΅Π½ΠΈΠΉ.
ΠΠΠ’ — ΠΠ±-Π°Π»ΠΊΠΈΠ»Π³ΡΠ°Π½ΠΈΠ΄ΠΈΠ½-ΠΠΠ Π°Π»ΠΊΠΈΠ»ΡΡΠ°Π½ΡΡΠ΅ΡΠ°Π·Π°, ΠΠΠ€Π — 2,4-Π΄ΠΈΠ½ΠΈΡΡΠΎΡΠ΅Π½ΠΈΠ»Π³ΠΈΠ΄ΡΠ°Π·ΠΈΠ½, ΠΠ’Π’ — Π΄ΠΈΡΠΈΠΎΡΡΠ΅ΠΈΡΠΎΠ»,.
ΠΠΠΠ-ΡΠ΅Π»Π»ΡΠ»ΠΎΠ·Π° — Π΄ΠΈΡΡΠΈΠ»Π°ΠΌΠΈΠ½ΠΎΡΡΠΈΠ» ΡΠ΅Π»Π»ΡΠ»ΠΎΠ·Π°, ΠΠΠ — Π»Π°ΠΊΡΠ°ΡΠ΄Π΅Π³ΠΈΠ΄ΡΠΎΠ³ΠΈΠ½Π°Π·Π° ΡΠΈΠΏ II ΠΈΠ· ΠΌΡΡΡΡ ΠΊΡΠΎΠ»ΠΈΠΊΠ°, ΠΠΠΠ — ΠΏΠΎΠ»ΠΈΠ°ΠΊΡΠΈΠ»Π°ΠΌΠΈΠ΄Π½ΡΠΉ Π³Π΅Π»Ρ, ΠΠΠ€ — ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Ρ-5'-ΡΠΎΡΡΠ°Ρ,.
ΠΠΠ ΠΠΠ— ΠΏΠΎΠ»ΠΈΡΡΠΈΠ»Π΅Π½ Π³Π»ΠΈΠΊΠΎΠ»Ρ ΠΌΠΎΠ½ΠΎΠΌΠ΅ΡΠΈΠ»ΠΎΠ²ΡΠΉ ΡΡΠΈΡ,.
5−10 Π’ΠΠ€ — N5-N10-ΠΌΠ΅ΡΠΈΠ»Π΅Π½-ΡΠ΅ΡΡΠ°Π³ΠΈΠ΄ΡΠΎΡΠΎΠ»Π°Ρ.
Π€ΠΠ‘Π€ — ΡΠ΅Π½ΠΈΠ»ΠΌΠ΅ΡΠΈΠ»-ΡΡΠ»ΡΡΠΎΠ½ΠΈΠ»ΡΡΠΎΡΠΈΠ΄,.
Π₯ΠΠΠ — Ρ Π»ΠΎΡΡΡΠΈΠ»Π½ΠΈΡΡΠΎΠ·ΠΎΠΌΠΎΡΠ΅Π²ΠΈΠ½Π°,.
ΠΠΠ’Π — ΡΡΠΈΠ»Π΅Π½Π΄ΠΈΠ°ΠΌΠΈΠ½ΡΠ΅ΡΡΠ°ΡΠΊΡΡΡΠ½Π°Ρ ΠΊΠΈΡΠ»ΠΎΡΠ°,.
LB-ΡΡΠ΅Π΄Π° — Lauria-Bertani ΡΡΠ΅Π΄Π°,.
NADH — Π½ΠΈΠΊΠΎΡΠΈΠ½Π°ΠΌΠΈΠ΄ Π°Π΄Π΅Π½ΠΈΠ½ Π΄ΠΈΠ½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄ ΡΠΎΡΡΠ°Ρ, Π²ΠΎΡΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½Π½Π°Ρ ΡΠΎΡΠΌΠ°, rMGL — ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Π°, ΡΠ΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΡΠΉ ΡΠ΅ΡΠΌΠ΅Π½Ρ.
ΠΠ±Π·ΠΎΡ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ.
ΠΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Π°. ΠΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅ΠΌΡΡ ΡΠ΅Π°ΠΊΡΠΈΠΉ, ΡΡΡΡΠΊΡΡΡΠ° ΠΈ ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ Π² ΠΌΠ΅Π΄ΠΈΡΠΈΠ½Π΅.
ΠΡΠ²ΠΎΠ΄Ρ.
1. Π Π°Π·ΡΠ°Π±ΠΎΡΠ°Π½ ΠΌΠ΅ΡΠΎΠ΄ ΠΎΡΠΈΡΡΠΊΠΈ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ ΠΈΠ· ΠΊΠ»Π΅ΡΠΎΠΊ Citrobacter freundii.
2. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½Π° Π½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄Π½Π°Ρ ΠΏΠΎΡΠ»Π΅Π΄ΠΎΠ²Π°ΡΠ΅Π»ΡΠ½ΠΎΡΡΡ ΡΡΠ°Π³ΠΌΠ΅Π½ΡΠ° Ρ ΡΠΎΠΌΠΎΡΠΎΠΌΡ Citrobacter freundii, ΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠ°Ρ Π³Π΅Π½, ΠΊΠΎΠ΄ΠΈΡΡΡΡΠΈΠΉ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ. ΠΠ»Ρ ΡΡΠΏΠ΅ΡΠΏΡΠΎΠ΄ΡΠΊΡΠΈΠΈ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ Citrobacter freundii ΡΠΊΠΎΠ½ΡΡΡΡΠΈΡΠΎΠ²Π°Π½Π° Π³ΠΈΠ±ΡΠΈΠ΄Π½Π°Ρ ΠΏΠ»Π°Π·ΠΌΠΈΠ΄Π° pET-mgl. Π Π΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°ΡΠ½ΡΠΉ ΡΠ΅ΡΠΌΠ΅Π½Ρ ΠΏΠΎΠ»ΡΡΠ΅Π½ Π² Π³ΠΎΠΌΠΎΠ³Π΅Π½Π½ΠΎΠΌ Π²ΠΈΠ΄Π΅.
3. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½Ρ ΠΊΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΡ ΡΠ΅Π°ΠΊΡΠΈΠΉ Π°, ΡΠΈ ΠΎΡ, (3-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΡΡΠ΄Π° ΡΡΠ±ΡΡΡΠ°ΡΠΎΠ² Π΄Π»Ρ ΡΠ½Π΄ΠΎΠ³Π΅Π½Π½ΠΎΠ³ΠΎ ΠΈ ΡΠ΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΠΎΠ³ΠΎ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ². Π£ΡΡΠ°Π½ΠΎΠ²Π»Π΅Π½Ρ Π·Π°ΠΌΠ΅ΡΠ½ΡΠ΅ ΡΠ°Π·Π»ΠΈΡΠΈΡ ΠΏΠΎΠ»ΡΡΠ΅Π½Π½ΡΡ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΠΎΠ² kcat ΠΈ ΠΠΌ ΠΎΡ Π°Π½Π°Π»ΠΎΠ³ΠΈΡΠ½ΡΡ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΠΎΠ² Π΄Π»Ρ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ ΠΈΠ· Π΄ΡΡΠ³ΠΈΡ ΠΈΡΡΠΎΡΠ½ΠΈΠΊΠΎΠ².
4. ΠΠ·ΡΡΠ΅Π½Ρ ΡΠΏΠ΅ΠΊΡΡΡ ΠΏΠΎΠ³Π»ΠΎΡΠ΅Π½ΠΈΡ ΠΈ ΠΊΡΡΠ³ΠΎΠ²ΠΎΠ³ΠΎ Π΄ΠΈΡ ΡΠΎΠΈΠ·ΠΌΠ° Ρ ΠΎΠ»ΠΎΡΠ΅ΡΠΌΠ΅Π½ΡΠ°. ΠΠΎΠΊΠ°Π·Π°Π½ΠΎ, ΡΡΠΎ Π²Π½ΡΡΡΠ΅Π½Π½ΠΈΠΉ Π°Π»ΡΠ΄ΠΈΠΌΠΈΠ½ ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ Π² ΠΎΠ±Π»Π°ΡΡΠΈ Π·Π½Π°ΡΠ΅Π½ΠΈΠΉ ΡΠ 6,0−8,0 ΡΡΡΠ΅ΡΡΠ²ΡΠ΅Ρ Π² ΠΎΠ΄Π½ΠΎΠΉ ΠΈΠΎΠ½Π½ΠΎΠΉ ΡΠΎΡΠΌΠ΅, Π² ΠΊΠΎΡΠΎΡΠΎΠΉ ΠΏΡΠ΅ΠΎΠ±Π»Π°Π΄Π°ΡΡΠΈΠΌ ΡΠ²Π»ΡΠ΅ΡΡΡ ΡΠ°ΡΡΠΎΠΌΠ΅Ρ ΠΊΠ΅ΡΠΈΠΌΠΈΠ½Π°.
5. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½Π° ΡΠ-Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡΡ ΡΠ΅Π°ΠΊΡΠΈΠΈ Π°, Ρ-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ L-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½Π° ΠΈ ΠΏΡΠ΅Π΄Π»ΠΎΠΆΠ΅Π½Π° ΠΊΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠ°Ρ ΡΡ Π΅ΠΌΠ° ΡΠ΅Π°ΠΊΡΠΈΠΈ. ΠΠ°Π½Π½ΡΠ΅ ΡΡΠ΅Ρ ΡΠΈΠΏΠΎΠ² ΠΊΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΡ ΠΈΠ·ΠΎΡΠΎΠΏΠ½ΡΡ ΡΡΡΠ΅ΠΊΡΠΎΠ² ΡΠ΅Π°ΠΊΡΠΈΠΈ Π°, Ρ-ΡΠ»ΠΈΠΌΠΈΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ L-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½Π° ΠΏΠΎΠΊΠ°Π·Π°Π»ΠΈ, ΡΡΠΎ ΡΡΠ°Π΄ΠΈΠΈ ΠΎΡΡΡΠ²Π° ΠΏΡΠΎΡΠΎΠ½ΠΎΠ² ΠΎΡ Π°ΠΈ |3-Π°ΡΠΎΠΌΠΎΠ² ΡΠ³Π»Π΅ΡΠΎΠ΄Π° Π½Π΅ ΡΠ²Π»ΡΡΡΡΡ ΡΠΊΠΎΡΠΎΡΡΡ-Π»ΠΈΠΌΠΈΡΠΈΡΡΡΡΠΈΠΌΠΈ.
6. ΠΠΎΠ΄ΠΎΠ±ΡΠ°Π½Ρ ΡΡΠ»ΠΎΠ²ΠΈΡ ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΡ ΠΊΡΠΈΡΡΠ°Π»Π»ΠΎΠ² ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ Citrobacter freundii, ΠΏΡΠΈΠ³ΠΎΠ΄Π½ΡΡ Π΄Π»Ρ ΡΠ΅Π½ΡΠ³Π΅Π½ΠΎΡΡΡΡΠΊΡΡΡΠ½ΠΎΠ³ΠΎ Π°Π½Π°Π»ΠΈΠ·Π°. ΠΠΎΠ»ΡΡΠ΅Π½Ρ ΠΊΡΠΈΡΡΠ°Π»Π»Ρ, ΠΏΠΎΠ·Π²ΠΎΠ»ΠΈΠ²ΡΠΈΠ΅ ΠΎΠΏΡΠ΅Π΄Π΅Π»ΠΈΡΡ ΠΏΡΠΎΡΡΡΠ°Π½ΡΡΠ²Π΅Π½Π½ΡΡ ΡΡΡΡΠΊΡΡΡΡ Ρ ΠΎΠ»ΠΎΡΠ΅ΡΠΌΠ΅Π½ΡΠ° Ρ ΡΠ°Π·ΡΠ΅ΡΠ΅Π½ΠΈΠ΅ΠΌ 1,9 Π.
ΠΠ°ΡΡΠΎΡΡΠ°Ρ ΡΠ°Π±ΠΎΡΠ° ΡΠΈΠ½Π°Π½ΡΠΎΠ²ΠΎ ΠΏΠΎΠ΄Π΄Π΅ΡΠΆΠ°Π½Π° Π³ΡΠ°Π½ΡΠ°ΠΌΠΈ Π ΠΎΡΡΠΈΠΉΡΠΊΠΎΠ³ΠΎ Π€ΠΎΠ½Π΄Π° ΡΡΠ½Π΄Π°ΠΌΠ΅Π½ΡΠ°Π»ΡΠ½ΡΡ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠΉ (№ 99−449 251, 02−04−48 010), Π³ΡΠ°Π½ΡΠΎΠΌ ΠΡΠ΅Π·ΠΈΠ΄Π΅Π½ΡΠ° Π Π€ ΠΏΠΎ ΠΏΠΎΠ΄Π΄Π΅ΡΠΆΠΊΠ΅ Π²Π΅Π΄ΡΡΠΈΡ Π½Π°ΡΡΠ½ΡΡ ΡΠΊΠΎΠ» ΠΠ¨-1800.2003.4.
ΠΠ²ΡΠΎΡ ΠΏΡΠΈΠ½ΠΎΡΠΈΡ Π±Π»Π°Π³ΠΎΠ΄Π°ΡΠ½ΠΎΡΡΡ Π΄.Ρ .Π½. Π’. Π. ΠΠ΅ΠΌΠΈΠ΄ΠΊΠΈΠ½ΠΎΠΉ Π·Π° Π½Π°ΡΡΠ½ΠΎΠ΅ ΡΡΠΊΠΎΠ²ΠΎΠ΄ΡΡΠ²ΠΎΡΠ»Π΅Π½-ΠΊΠΎΡ. Π ΠΠ, ΠΏΡΠΎΡ. Π. Π. ΠΠ°Π±ΠΈΠ±ΠΎΠ²Ρ Π·Π° ΡΡΠ°ΡΡΠΈΠ΅ Π² ΠΎΠ±ΡΡΠΆΠ΄Π΅Π½ΠΈΠΈ ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠΎΠ²ΠΊ.Ρ .Π½. A.M. ΠΡΠΈΡΡΠ½Ρ Π·Π° ΡΡΠ°ΡΡΠΈΠ΅ Π² ΠΎΠ±ΡΡΠΆΠ΄Π΅Π½ΠΈΠΈ ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠΎΠ²ΠΊ.Ρ .Π½. Π. Π. Π€Π°Π»Π΅Π΅Π²Ρ Π·Π° ΡΡΠ°ΡΡΠΈΠ΅ Π² ΡΠ°Π±ΠΎΡΠ΅, ΠΎΠ±ΡΡΠΆΠ΄Π΅Π½ΠΈΠΈ ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠΎΠ² ΠΈ ΡΠΈΠ½ΡΠ΅Π· [Π°HJ-L-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½Π°- [ΡΡ, Π , Π Π3]-Π¬-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½Π°ΠΏΡΠΎΡ. Π. Π. ΠΠ°Π²ΠΈΠ»ΡΠ³Π΅Π»ΡΡΠΊΠΎΠΌΡ, ΠΊ.Π±.Π½. Π. ΠΠ°Π½ΡΡ ΠΎΠ²Ρ, ΠΊ.Π±.Π½. Π‘. Π Π°ΡΡΠΎΡΠ³ΡΠ΅Π²Ρ Π·Π° ΡΡΠ°ΡΡΠΈΠ΅ Π² ΡΠ°Π±ΠΎΡΠ΅ ΠΏΠΎ ΠΊΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΠΏΡΠΎΡ. Π. Π. ΠΠ°ΡΠ±Π΅Ρ, ΠΊ.Π±.Π½. Π. Π. ΠΠΈΠΊΡΠ»ΠΈΠ½Ρ, ΠΊ.Ρ .Π½. Π‘. Π. Π Π΅Π²ΡΠΎΠ²ΠΈΡ,* ΠΊ.Π±.Π½. Π‘. Π. ΠΠΈΠΊΠΎΠ½ΠΎΠ²Ρ Π·Π° Π°ΠΊΡΠΈΠ²Π½ΠΎΠ΅ ΡΡΠ°ΡΡΠΈΠ΅ Π² ΡΠ°ΡΡΠΈΡΡΠΎΠ²ΠΊΠ΅ ΠΊΡΠΈΡΡΠ°Π»Π»ΠΈΡΠ΅ΡΠΊΠΎΠΉ ΡΡΡΡΠΊΡΡΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΠΊ.Ρ.ΠΌ.Π½. Π. Π. ΠΠ°ΠΆΡΠ»ΠΈΠ½ΠΎΠΉ Π·Π° ΠΎΠ±ΡΠ°Π±ΠΎΡΠΊΡ ΠΈ ΠΎΠ±ΡΡΠΆΠ΄Π΅Π½ΠΈΠ΅ ΡΠΏΠ΅ΠΊΡΡΠ°Π»ΡΠ½ΡΡ Π΄Π°Π½Π½ΡΡ ΠΏΡΠΎΡ. Π. Π‘. ΠΠ½Π΄ΡΠ΅Π΅Π²ΠΎΠΉ Π·Π° ΠΏΠΎΠΌΠΎΡΡ Π² ΠΏΠΎΠ΄Π³ΠΎΡΠΎΠ²ΠΊΠ΅ ΡΠ΅ΠΊΡΡΠ° Π΄ΠΈΡΡΠ΅ΡΡΠ°ΡΠΈΠΈΠ.Π.Π‘ΠΈΠ½ΠΈΡΡΠ½ΠΎΠΉ ΠΈ ΠΊ.Ρ .Π½. Π. Π. ΠΠ°ΠΊΠΎΠΌΡΡΠ΄ΠΈΠ½ΠΎΠΉ Π·Π° ΡΡΠ°ΡΡΠΈΠ΅ Π² ΡΠ°Π±ΠΎΡΠ΅ΠΊ.Ρ .Π½. Π. Π. ΠΠ°ΡΠ±ΠΎΠ»ΠΈΠ½ΠΎΠΉ Π·Π° ΡΡΠ°ΡΡΠΈΠ΅ Π² ΡΠ°Π±ΠΎΡΠ΅ ΠΏΠΎ ΠΊΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΈ Π² ΠΎΠ±ΡΡΠΆΠ΄Π΅Π½ΠΈΠΈ ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠΎΠ²ΠΊ.Ρ .Π½. Π. Π. ΠΡΠ»ΠΈΠΊΠΎΠ²ΠΎΠΉ Π·Π° ΠΊΡΠΈΡΠΈΡΠ΅ΡΠΊΠΎΠ΅ ΡΡΠ΅Π½ΠΈΠ΅ ΡΡΠΊΠΎΠΏΠΈΡΠΈ ΠΈ ΠΏΠΎΠΌΠΎΡΡ Π² ΠΏΠΎΠ΄Π³ΠΎΡΠΎΠ²ΠΊΠ΅ ΡΠ΅ΠΊΡΡΠ° Π΄ΠΈΡΡΠ΅ΡΡΠ°ΡΠΈΠΈΠΊ.Ρ .Π½. Π. Π. ΠΠΈΠΊΠΈΡΠΈΠ½Ρ Π·Π° ΠΊΡΠΈΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ Π·Π°ΠΌΠ΅ΡΠ°Π½ΠΈΡ ΠΈ ΠΏΠΎΠΌΠΎΡΡ Π² ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΠΈ ΡΠΎΡΠΎΠ³ΡΠ°ΡΠΈΠΉ ΠΊΡΠΈΡΡΠ°Π»Π»ΠΎΠ² ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°ΡΠΎΡΡΡΠ΄Π½ΠΈΠΊΠ°ΠΌ Π»Π°Π±ΠΎΡΠ°ΡΠΎΡΠΈΠΈ Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΡ ΠΎΡΠ½ΠΎΠ² Π±ΠΈΠΎΠΊΠ°ΡΠ°Π»ΠΈΠ·Π° ΠΈ Π²ΡΠ΅ΠΌ ΡΠΎΡΡΡΠ΄Π½ΠΈΠΊΠ°ΠΌ ΠΠΠ Π ΠΠ Π·Π° ΠΏΠΎΠΌΠΎΡΡ Π² ΡΠ°Π±ΠΎΡΠ΅.
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- Gyorgy P. The history of vitamin B6. I/The American journal of clinical nutrition, 1956, v.4, 4, p.313−317.
- Umbreit W.W. and Gunsalus I.C. The function of pyridoxine derivatives: arginine and glutamic acid decarboxylases. IIJ Biol Chem, 1945, v. 159, p.333−341.
- ΠΠ΅ΡΠ»Π΅Ρ Π. ΠΠΈΠΎΡ ΠΈΠΌΠΈΡ. Π₯ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠ΅Π°ΠΊΡΠΈΠΈ Π² ΠΆΠΈΠ²ΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠ΅. Π., ΠΠΈΡ, 1980, Ρ.2, Ρ. 75.
- John R.A. Pyridoxal phosphate-dependent enzymes. Review. IIBiochimica et Biophysica Acta, 1995, v.1248, 2, p.81−96.
- ΠΡΠ°ΡΠΈΡΡΠ΅ΠΉΠΈ A.E., Π¨Π΅ΠΌΡΠΊΠΈΠ½ M.M. Π’Π΅ΠΎΡΠΈΡ ΠΏΡΠΎΡΠ΅ΡΡΠΎΠ² Π°ΠΌΠΈΠ½ΠΎΠΊΠΈΡΠ»ΠΎΡΠ½ΠΎΠ³ΠΎ ΠΎΠ±ΠΌΠ΅Π½Π°, ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅ΠΌΡΡ ΠΏΠΈΡΠΈΠ΄ΠΎΠΊΡΠ°Π»Π΅Π²ΡΠΌΠΈ ΡΠ½Π·ΠΈΠΌΠ°ΠΌΠΈ. //ΠΠΈΠΎΡ ΠΈΠΌΠΈΡ, 1953, Ρ. 18, Ρ. 393−411.
- Metzler, D.E., Ikawa, Π., and Snell- Π.Π., Transamination of Pyridoxamine and Amino Acids with Glyoxylic Acid. //J.Amer.Chem.Soc., 1954, 76, 644−648.
- Clausen Π’., Laber B. and Messerschmidt A. Mode of action of cystathionine (3-lyase. //Biol. Chem., 1997, v. 378, p. 321−326.
- Dunathan H.C. Conformation and reaction specificity in pyridoxal phosphate enzymes. UProc. Natl. Acad. Sci. USA, 1966, 55, 712−716.
- Eliot A.C. & Kirsch J.F. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. HAnnu. Rev. Biochem., 2004, v.73, p.383−415.
- Ivanov V.I. & Karpeisky M.Ya. Dynamic three-dimensional model for enzymic transamination. //Adv. Enzymol. Relat. Areas Mol. Biol. 1969, 32, 21−53.
- Enzyme Nomenclature, Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. Acad. Press, 2002.
- Tanaka H., Esaki N., Soda K. A versatile bacterial enzyme: L-methionine y-lyase. //Enzyme Microb. Technol., 1985, v. 7, p.530−537.
- Tanaka H., Esaki N., Soda K. Synthesis of optically active sulfur and selenium amino acids with microbial enzymes. HAppl. Biochem. Biotechnol. 1985, 11 71−82.
- Alexander F.W., Sandmeier E., Mehta P.K., Christen P. Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes: regio-specific a, P and y-families. //Eur. J. Biochem., 1994, v. 219, p. 953−960.
- Kreis W., Hession C. Isolation and purification of L-methionine-alpha-deamino-mercaptomethane-lyase (L-methioninase) from Clostridium sporogenes. //Cancer Res 1973, 33, 1862−1865
- ΠΡΠΊΠΈΠ½Π° Π.Π., ΠΠ΅ΡΠ΅Π·ΠΎΠ² Π’. Π’., ΠΠ°Π½ΠΈΠ½ Π. Π. Π¨ΡΠ°ΠΌΠΌ Pseudomonas taetrolens ΠΠΠΠ-904 ΠΏΡΠΎΠ΄ΡΡΠ΅Π½Ρ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ° ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½Π°Π·Ρ: ΠΠ²ΡΠΎΡΡΠΊΠΎΠ΅ ΡΠ²ΠΈΠ΄Π΅ΡΠ΅Π»ΡΡΡΠ²ΠΎ 967 077, 1982.
- Nakayama Π’., Esaki N., Lee W.J., Tanaka I., Tanaka H., Soda Π., Purification and properties of L-methionine y-lyase from Aeromonas sp. l/Agric. Biol. Chem., 1984, v. 48, p. 2367−2369.
- Esaki N., Soda K. L-methionine gamma-lyase from Pseudomonas putida and Aeromonas. //Methods Enzymol., 1987, v. 143, p. 459−465.
- Kobayashi Π’., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu Π’., Koike K., Kawai S. and Ito S. Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16 HAppl. Microbiol. Biotechnol., 1995, v. 43 (3), p. 473−481.
- Faleev N.G., Troitskaya M.V., Paskonova E.A., Saporovskaya M.B., Belikov V.M. L-Methionine y-lyase in Citrobacter intermedius cells: Stereochemical requirements with respect to the tiol structure. //Enzyme Microb. Technol., 1996, v. 19, p. 590−593.
- Tanaka H., Esaki N., Soda K. Properties of L-methionine gamma-lyase from Pseudomonas ovalis. //Biochemistry, 1977, v. 16, p. 100 106.
- Dias Π., Weimer B. Purification and characterization of L-methionine y-lyase from Brevibacterium lines B12. HAppl. Environ. Microbiol., 1998, v. 64 (9), p. 3327−3331.
- Yoshimura M., Nakano Y., Yamashita Y., Oho Π’., Saito Π’., Koga T. Formation of methyl mercaptan from L-methionine by Porphyromonas gingivalis. //Infect. Immun. 2000, v. 68, p. 6912−6916.
- Yoshimura M., Nakano Y., Fukamachi H., Koga T. 3-Chloro-DL-alanine resistance by L-methionine-alpha-deamino-gamma-mercaptomethane-lyase activity. IIFEBS Lett., 2002, v. 523(1−3), p. 119−122.
- Takami H., Takaki Y., Uchiyama I. Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments. //Nucleic Acids Res., 2002, v. 30 (18), p. 3927−3935.
- Tokoro M., Asai Π’., Kobayashi S., Takeuchi Π’., and Nozaki T. Identification and characterization of two isoenzymes of methionine y-lyase from Entamoeba histolytica. IIJ. Biol. Chem., 2003, v. 278, p. 42 717−42 727.
- Daraselia N., Dernovoy D., Tian Y., Borodovsky M., Tatusov R., Tatusova T. Reannotation of Shewanella oneidensis genome. HOMICS, 2003, v. 7 (2), p. 171−175.
- Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E. and Tice H. //Direct Submission, ENTREZ, Proteins, ACCESSION YP085976.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION YP603484.
- Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran Π., Rogers Y.-H., Friedman R. and Venter J.C. //Direct Submission, Proteins, ACCESSION YP458784.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION ZP00606108.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission ENTREZ, Proteins, ACCESSION YP525366.
- Copeland A., Lucas- S., Lapidus A., Barry K., Detter J.C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION YP484072.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION ZP00587584.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION ZP01435953.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina i Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION YP563524.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION YP750060.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION YP738587.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P: //Direct Submission, ENTREZ, Proteins, ACCESSION ZP00815415.
- Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina Π’., Hammon N., Israni S., Pitluck S. and Richardson P. //Direct Submission, ENTREZ, Proteins, ACCESSION YP614731.
- Fukamachi H., Nakano Y., Okano S., Shibata Y., Abiko Y., Yamashita Y. High production of methyl mercaptan by L-methionine-alpha-deamino-gamma-mercaptomethane lyase from Treponema denticola. /1Biochem. Biophys. Res. Commun., 2005, v. 331(1), p. 127 131. i
- Esaki N., Suzuki Π’., Tanaka H., Soda K., Rando R.R. Deamination and gamma-addition reactions of vinylglycine by L-methionine gamma-lyase. //FEBS Lett., 1977, v. 84 (2), p. 309−312.
- Johnston M., Jankowski D., Marcotte P., Tanaka H., Esaki N., Soda K. and Walsh Ch. Suicide inactivation of bacterial cystathionine y-synthase and methionine y-lyase during processing of propargylglycine. //Biochemistry, 1979, v. 18, p. 4690−4701.
- Johnston M., Raines R, Chang M., Esaki N., Soda K., Walsh C. Mechanistic studies on reactions of bacterial methionine gamma-lyase with olefinic amino acids. //Biochemistry, 1981, v. 20 (15), p. 43 254 333.
- Esaki N., Nakayama Π’., Sawada S., Tanaka H., Soda K. !H NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine gamma-lyase. //Biochemistry, 1985, v. 24 (15), p. 38 573 862.
- Inoue H., Inagaki K., Adachi N., Tamura Π’., Esaki N., Soda K. and Tanaka H. Role of Tyrosine 114 of L-methionine y-lyase from Pseudomonas putida. UBiosci. Biotechnol. Biochem., 2000, v. 64 (11), p. 2336−2343.
- Christen P., Mehta P.K. From cofactor to enzymes. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes. Review. HChem Rec., 2001, v. 1 (6), p. 436−447.
- Johnston M., Marcotte P., Donovan J., Walsh C. Mechanistic studies with vinylglycine and beta-haloaminobutyrates as substrates for cystathionine gamma-synthetase from Salmonella typhimurium. IIBiochemistry, 1979, v. 18, p. 1729−1738.
- Guggenheim S. and Flavin M. Cystathionine gamma-synthase from Salmonella. //J. Biol. Chem., 1971, v. 246, p. 3562−3568.
- Silverman R.B., Abeles R.H. Mechanism of inactivation of gamma-cystathionase by beta, beta, beta trifluoroalanine. 11 Biochemistry, 1977, v. 16 (25), p. 5515−5520.
- Lockwood B.C. and Coombs G.H. Purification and characterization of methionine y-lyase from Trichomonas vaginalis. 11 Biochem. J., 1991, v. 279, p. 675−682.
- Tanaka H., Esaki N., Yamamoto Π’., Soda K. Purification and properties of methioninase from Pseudomonas ovalis. IIFEBS Letters, 1976, v. 66, p.307−311.
- Flavin M. and Guggenheim S., in Yamada K., Katunuma N. and Wada H. (Editors), Symposium on pyridoxal enzymes, Maruzen Company, Ltd., Tokyo, 1968, p.89.
- Davis L., and Metzler D.E. Pyridoxal-linked elimination and replacement reactions. In: The Enzymes (3rd Ed.) Ed. Boyer P.D., Wiley and Sons, N.Y., 1972, v. 3, p. 33−74.
- Kallen R.G., Korpela Π’., Martell A.E. Matsushima Y., Metzler C.M., Metzler D.E. Morozov Y.V., Ralston I.M., Savin F.A., Torchinsky Y.M. & Ueno H. The Transaminases, New York, Wiley, 1985, p. 37−105.
- Karube Y. and Matsushima Y. A model for an intermediate in pyridoxal catalyzed gamma-elimination and gamma-replacement reactions of amino acids. IIJ. Am. Chem. Soc., 1977, v. 99, p. 13 561 358. β’
- Metzler D.E., Harris C.M., Johnston R.J., Siano D.B. & Thomson J.A. Spectra of 3-hydroxypyridines. Band-shape analysis and evaluation of tautomeric equilibria. ΠBiochemistry, 1973, v. 12, p. 5377−5392.
- Walsh C. Enzymatic Reaction Mechanism- Freeman, San Francisco, 1979, p. 777−827.
- Posner B.I. & Flavin M. Cystathionine-synthase. The nature of intramolecular proton shifts in the elimination reaction. IIJ. Biol. Chem., 1972, v. 247, p. 6412−6419.
- Jansonius J.N. Structure, evolution and action of vitamin B6-dependent enzymes. //Curr. Opin. Struct. Biol., 1998, v. 8(6), p. 75 969. Review.
- Grishin N.V., Phillips M.A., Goldsmith E.J. Modeling of the spatial structure of eukaryotic ornithine decarboxylases. //Protein Sci., 1995, v. 4(7), p. 1291−1304.
- Qu K., Martin D.L., Lawrence C.E. Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase. //Protein ScL, 1998, v. 7(5), p. 1092−1105.
- Revtovich S.V., Mamaeva D.V., Morozova E.A., Nikulin A.D., Nikonov S.V., Garber M.B., Demidkina T.V. Crystal Sructure of Citrobacter freundii L-methionine-lyase, 2004, PDB: 1Y4I.
- Sato D., Yamagata W., Kamei K., Nozaki Π’., Harada S. Expression, purification and crystallization of L-methionine gamma-lyase 2 from Entamoeba histolytica. IIActa Crystallograph. Sect. F Struct. Biol. Cryst. Commun., 2006, v. 62, p. 1034−1036.
- Clausen Π’., Huber R., Laber Π., Pohlenz H., and Messerchmidt A Crystal structure of pyridoxal 5'-phosphate dependent cystathionine (3-lyase from E. Coli at 1.83 A. IIJ. Mol. Biol., 1996, v. 262, p. 202 -224.
- Kack H., Sandmark J., Gibson K., Schneider G., Lindqvist Y. Crystal structure of diaminopelargonic acid synthase: evolutionaryrelationships between pyridoxal-5'-phosphate-dependent enzymes. //J. Mol. Biol., 1999, v. 291(4), p. 857−876.
- Mamaeva D.V., Morozova E.A., Nikulin A.D., Revtovich S.V., Nikonov S.V., Garber M.B., and Demidkina T.V. Structure of Citrobacter freundii L-methionine gammarlyase. HActa Crystallograph. Sect. F Struct. Biol. Cryst. Commun., 2005, v. 61, p.546.549.
- Tanaka H., Yamada H., Esaki N., Soda K. Selective determination of L-methionine and L-cysteine with bacterial L-methionine y-lyase and antitumor activity of the enzyme. IIJ. Appl. Biochem., 1980, v. 2, p. 439−444.
- Fung K.W., Kuan S.S., Sung H.Y., Guilbault G.G. Methionine selective enzyme electrode. 11 Anal. Chem., 1979, v. 51, p. 2319−2324.
- Yoshimura M., Nakano Y., Koga T. L-Methionine-gamma-lyase, as a target to inhibit malodorous bacterial growth by trifluoromethionine. 11 Biochem. Biophys. Res. Commun., 2002, v.292(4), p. 964−968.
- Nakano Y., Yoshimura M., Koga T. Methyl mercaptan production by periodontal bacteria. Hint. Dent. J., 2002, v. 3, p. 217−220.
- Arfi K., Amarita F., Spinnler H.E., Bonnarme P. Catabolism of volatile sulfur compounds precursors by Brevibacterium linens and Geotrichum candidum, two microorganisms of the cheese ecosystem. IIJ Biotechnol., 2003, v. 105(3), p. 245−253.
- Bonnarme P., Lapadatescu C., Yvon M., Spinnler H.E. L-methionine degradation potentialities of cheese-ripeningmicroorganisms. IIJ Dairy Res., 2001, v. 68(4), p. 663−674.
- Amarita F., Requena Π’., Taborda G., Amigo L., Pelaez C. Lactobacillus casei and Lactobacillus plantarum initiate catabolism of methionine by transamination. IIAppl Microbiol., 2001, v. 90(6), p. 971−978.
- Bonnarme P., Psoni L., Spinnler H.E. Diversity of L-methionine catabolism pathways in cheese-ripening bacteria. IIAppl Environ Microbiol., 2000, v. 66(12), p. 5514−5517.
- Dias Π., Weimer B. Conversion of methionine to thiols by lactococci, lactotiacilli, and- brevibacteria. IIAppl Environ Microbiol., 1998, v. 64(9), p. 3320−3326.
- Weimer Π., Seefeldt K., Dias B. Sulfur metabolism in bacteria associated3 with cheese. Review. IIAntonie Van Leeuwenhoek., 1999, v. 76(1−4), p. 247−261.
- Hoffman R.M. Methioninase: A therapeutic for diseases, related-to altered-methionine metabolism and transmethylation: cancer, heart disease, obesity, aging, and Parkinson’s disease. Ulluman Cell, 1 997, v. 10, p. 69−80.
- Cellarier E., Durando X., Vasson M.P., Farges M.C., Demiden A., Maurizis J.C., Madelmont J: C. and Chollet P. 11 Cancer Treat Rev., 2003, v. 29, p. 489−499.
- Jones P.A. Death and methylation. //Nature, 2001, v. 409, p. 141 144.
- Breillout F., Antoine E., Poupon M.F. Methionine dependency of malignant tumors: a possible approach for therapy. IIJ Natl Cancer Inst., 1990, v. 82, p. 1628−1632.
- Hoffman R.M. Altered methionine metabolism and transmethylation in cancer. IIAnticancer Res., 1985, v. 5, p. 1−30.
- Kokkinakis D.M., Hoffman R.M. Frenkel E.P., et al. Synergy between methionine stress and chemotherapy in the treatment of brain tumor xenografts in athymic mice. 11 Cancer Res., 2001, v. 61, p. 40 174 023.
- Poirson-Bichat F., Goncalves RA, Miccoli L., Dutrillaux Π., Poupon MF. Methionine depletion enhances the antitumoral efficacy of cytotoxic agents in drug-resistant human tumor xenografts. HClin. Cancer Res., 2000, v. 6, p. 643−653.
- Guo HY, Herrera H., Groce A., Hoffman RM, Expression of the biochemical defect of methionine dependence in fresh patient tumors in primary histoculture. 11 Cancer Res., 1993, v. 53, p. 2479−2483.
- Halpern B.C., Clark B.R., Hardy D.N., Halpern R.M., Smith R.A. The effect of remplacement of methionine by homocysteine on survival of malignant and normal adult mammalian cells in culture. I/Proc. Natl. Acad. Sci. USA, 1974, v. 71, p. 1 133−1 136.
- Stern P.H., Hoffman R.M. Enhanced in vitro selective toxicity of chemotherapeutic agents for human cancer cells based on a metabolic defect. HJ. Natl. Cancer Inst., 1986, v. 76, p. 629−639.
- Hoffman R.M. Methionine dependence in cancer cells A review. Illn Vitro, 1982, v. 18, p. 421−428.
- Kreis W., Baker A., Ryan V., Bertasso A. Effect of nutritional and enzymatic methionine deprivation upon human normal and malignant cells in tissue culture. I/Cancer Res., 1980, v. 40, p. 634 641.
- Mecham J.O., Rowitch D., Wallace C.D. Stern P.H., Hoffman R.M. The methabolic defect of methionine dependence occurs frequently in human tumor cell lines. //Biochem Biophys Res Commun, 1983, v. 117, p.429−434.
- Ashe H., Clark BR, Chu F., et al. N5-methyltetrahydrofolate: homocisteine methyltransferase activity in extracts from normal, malignant and embryonic tissue culture cells. IIBiochem Biophys Res Commun., 1974, v. 57, p. 417−425.
- Poirier L.A., Wilson M.J. The elevated requirement for methionine by transformed rat liver epithelial cells in vitro. IIAnn N Y Acad Sci., 1980, v. 349, p. 283−293.
- Kenyon S.H., Waterfield C.J., Timbrell J.A., Nicolaou A. Methionine synthase activity and sulphur amino acid levels in the rat liver tumor cells HTC and Phi-1. IIBiochem Pharmacol., 2000, v. 63, p. 381−391.
- Judde J.G., Ellis M., Frost P. Biochemical analysis of the role of transmethylation in the methionine dependence of tumor- cells. //Cancer Res., 1989, v. 49, p. 4859−4865.
- Liteplo R.G., Hipwell S.E., Rosenblatt D.S., Sillaots S., Lue-Shing H. Changes in cobalamin metabolism are associated with the altered methionine auxotrophy of highly growth autonomous human melanoma cells. HJ Cell Physiol, 1991, v. 149, p. 332−338.
- Fiskerstrand Π’., Christensen Π., Tysnes O.B., Ueland P.M., Refsum H. Development and reversion of methionine dependence in a human glioma cell line: relation to homocysteine remethylation and cobalamin status. HCancer Res., 1994, v. 54, p. 4899−4906.
- Jacobsen S.J., North J.A., Rao N.A., Mangum J.H. 5-Methyltetrahydrofolate: synthesis and utilization in normal and SV40transformed BHK-21 cells. UBiochem Biophys Res Commun, 1977, v. 76, p. 46−53.
- Frosst P., Blom H.J., Milos R., et al. A candidate genetic risk factor for vascular disease: a common mutation in methylentetrahydrofolate reductase. //Nat Genet, 1995, v. 10, p. 111 113.
- Van der Put N.M., Gabreels F., Stevens E.M., et al. A second common mutation in the methylentetrahydrofolate reductase gene: an additional risk factor for neural-tube defects? //Am J Hum Genet, 1998, v. 62, p. 1044−1051.
- Bergstrom M., Ericson K., Hagenfeldt L., et al. PET study of methionine accumulation in glioma and normal brain tissue: competition with branched chain amino acids. HJ Comput Assist Tomogr, 1987, v. 11, p. 208−213.
- Zingg J.M., Jones P.A., Genetic and epigenetic aspects of DNA methylation on genome expression, evolution, mutation and carcinogenesis. //Carcinogenesis, 1997, v. 18, p. 869−882.
- Baylin S.B., Herman J.G., Graff J.R., Vertino P.M., Issa J.P. Alterations in DNA methylation: a fundemental aspect of neoplasia. HAdv Cancer Res., 1998, v. 72, p. 141−196.
- Dumontet C., Roch A.M., Quash G. Methionine dependence of tumor cells: programmed cell survival? //Oncol Res., 1996, v. 8, p. 469−471.
- Fitchen J.H., Riscoe M.K., Dana B.W., Lawrence H.J., Ferro A.J. Methylthioadenosine phosphorylase deficiency in human leukemias and solid tumors. //Cancer Res., 1986, v. 46, p. 5409−5412.
- Nobori Π’., Szinai I., Amox D., et al. Methylthioadenosine phosphorylase deficiency in human non-small cell lung cancers. //Cancer Res., 1993, v. 53, p. 1098−1101.
- Traweek S.T., Riscoe M.K., Ferro A.J., Braziel R.M., Magenis R.E., Fitchen J.H. Methylthioadenosine phosphorilase deficiency in acute leukemia: pathologic, cytogenetic, and clinical features. IIBlood, 1988, v. 71, p. 1568−1573.
- Nobori Π’., Karras J.G., Delia Ragione F., Waltz T.A., Chen P.P., Carson D.A. Absence of methylthyoadenosine phosphorylase in human gliomas. UCancer Res., 1991, v. 51, p. 3193−3197.
- Ogier G., Chantepie J., Deshayes C., et al. Contribution of 4-methylthio-2-oxobutanoate and its transaminase to the growth of methionine-dependent cells in culture. Effect of transaminase inhibitors. 11 Biochem Pharmacol,. 1993, v. 45, p. 1631−1644.
- Tang Π., Li Y.N., Kruger W.D. Defects in methylthioadenosine phosphorylase are associated with but not responsible for methionine-dependent tumor cell growth. UCancer Res., 2000, v. 60, p. 55 435 547.
- Kreis W., Hession C. Biological effects of enzymatic deprivationof L-methionine in cell culture and an experimental tumor. UCancer
- Res., 1973, v. 33, p. 1866−1869.
- Tan Y., Xu M., Guo H., Sun X., Kubota Π’., Hoffman RM. Anticancer efficacy of methioninase in vivo. //Anticancer Res., 1996, v. 16, p. 3931−3936.
- Hori H., Takabayashi K., Orvis L., Carson DA, Nobori Π’., Gene cloning and characterization of Pseudomonas putida L-methionine alpha-deamino-gamma-mercaptomethane-lyase. UCancer Res., 1996, v. 56, p. 2116−2122.
- Tan Y., Zavala Sr.J., Xu M., Zavala Jr. J, Hoffman RM. Serum methionine depletion without side effects by methioninase in metastatic breast cancer patients. 11 Anticancer Res., 1996, v. 16, p. 3937−3942.
- Tan Y., Zavala Sr.J., Han Q., et al. Recombinant methioninase infusion reduces the biochemical endpoint of serum methionine with minimal toxity in high-stage cancer patients. 11 Anticancer Res., 1997, v. 17, p. 3857−3860.
- Tan Y., Sun X., Xu M., An Z., Tan X., Han Q., Miljkovic D.A., Yang M., Hoffman R.M. Polyethilene glycol conjugation of recombinant methioninase for cancer therapy. UProtein Expr. Purif., 1998, v. 12 (1), p. 45−52.
- Miki K., Xu M., Gupta A., Ba Y., Tan Y., Al-Rafaie W., Bouvet M., Makuuchi M., Moossa A.R., Hoffman R.M. Methioninase cancer gene therapy with selenomethionine as suicide prodrug substrate. UCancer Res., 2001, v. 61, p.6805−6810.
- Peters G.J., Backus H.H., Freemantle S., et al. Induction of thymidylate synthase as a 5-fluorouracil resistance mechanism. IIBiochim. Biophys. Acta, 2002, v. 1587, p. 194−205.
- Thomas D.M., Zalcberg J.R. 5-Fluorouracil: a pharmacological paradigm in the use of cytotoxics. HClin Exp Pharmacol Physiol., 1998, v. 25, p. 887−895.
- Yoshioka Π’., Wada Π’., Uchida N., et al. Anticancer efficacy in vivo and in vitro, synergy with 5-fluorouracil, and safety of recombinant methioninase. //Cancer Res., 1998, v. 58, p. 2583−2587.
- Machover D., Zittoun J., Broet P., et al. Cytotoxic synergism of methioninase in combination with 5-fluorouracil and folinic acid. //Biochem Pharmacol., 2001, v., 61, p. 867−876.
- Gou H., Lishko V.K., Herrera H., Groce A., Kubota Π’., Hoffman R.M. Therapeutic tumor-specific cell cycle block induced by methionine starvation in vivo. //Cancer Res., 1993, v. 53, p. 56 765 679.
- Goseki N., Yamazaki S., Endo M., et al. Antitumor effect of methionine-depleting total parental nutrition with doxorubicin administration on Yoshida sarcoma-bearing rats. //Cancer, 1992, v. 69, p. 1865−1872.
- Kokkinakis D.M., von Wronski M.A., Vuong Π’.Π., Brent T.P., Schold Jr.S.C. Regulation of ΠΠ±-methylguanine-DNAmethyltransferase by methionine in human tumour cells J/Br.
- J.Cancer, 1997, v. 75, p. 779−788.
- Tan Y., Sun X., Xu M., et al. Efficacy of recombinant methioninase in combination with cisplatin on human colon tumors in nude mice. HClin. Cancer Res., 1999, v. 5, p. 2157−2163.
- Hoshiya Y., Kubota Π’., Matsuzaki S.W., Kitajima M., Hoffman R.M. Methionine starvation modulates the efficacy of cisplatin on human breast cancer in nude mice. //Anticancer Res., 1996, v. 16, p. 3515−3517.
- Technique de Chromatographie adaptees a la Purification des Proteines et des Macromolecules Biologiques. Formation GE Healthcare & CNRS, Montpellier, 2006.
- Π‘ΡΠ΅ΠΏΠ°Π½ΠΎΠ² Π.Π. ΠΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½Π°Ρ Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΡ. Π‘ΡΡΡΠΊΡΡΡΠ° ΠΈ ΡΡΠ½ΠΊΡΠΈΠΈ Π±Π΅Π»ΠΊΠΎΠ². ΠΠΎΠ΄ ΡΠ΅Π΄. Π°ΠΊ. Π. Π‘. Π‘ΠΏΠΈΡΠΈΠ½Π°, ΠΠΎΡΠΊΠ²Π°, «ΠΡΡΡΠ°Ρ ΡΠΊΠΎΠ»Π°», 1996, 334 Ρ.
- ΠΡΠΊΠΈΠ½Π° Π.Π. Π€ΠΈΠ·ΠΈΠΊΠΎ-Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΈ ΡΠ½Π·ΠΈΠΌΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠ²ΠΎΠΉΡΡΠ²Π° L-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ Ρ-Π»ΠΈΠ°Π·Ρ ΠΈΠ· Pseudomonas taetrolens: ΠΠ²ΡΠΎΡΠ΅Ρ. Π΄ΠΈΡ. Π½Π° ΡΠΎΠΈΡΠΊΠ°Π½ΠΈΠ΅ ΡΡΠ΅Π½ΠΎΠΉ ΡΡΠ΅ΠΏΠ΅Π½ΠΈ ΠΊΠ°Π½Π΄.Π±ΠΈΠΎΠ».Π½Π°ΡΠΊ. Π.: Π ΠΎΡΡΠΈΠΉΡΠΊΠΈΠΉ ΡΠ½ΠΈΠ²Π΅ΡΡΠΈΡΠ΅Ρ Π΄ΡΡΠΆΠ±Ρ Π½Π°ΡΠΎΠ΄ΠΎΠ², 1992.
- Nakayama Π’., Esaki N., Sugie Π., Beresov Π’.Π’., Tanaka Π., and Soda Π. Purification of bacterial L-methionine y-lyase. 11 Anal. Biochem., 1984, v. 138, p. 421−424.
- Tanaka H., Esaki N., Yamamoto T. and Soda K. Purification and properties of methioninase from Pseudomonas ovalis. IIFEBS Lett., 1976, v. 66 (2), p. 307−31 1.
- Ito S., Nakamura Π’., Eguchi Y. Purification and characterization of methioninase from Pseudomonas putida. //J. Biochemistry (Tokyo), 1976, v. 79, p. 1263 1272.
- Π‘ΠΊΠΎΡΠΏΡ P. ΠΠ΅ΡΠΎΠ΄Ρ ΠΎΡΠΈΡΡΠΊΠΈ Π±Π΅Π»ΠΊΠ°. M., ΠΠΈΡ, 1985.
- Tanaka Π., Esaki N., Soda Π. Bacterial L-methionine y-lyase: characterization and application. //Sulfur Amino Acids: Biochemical and Clinical Aspects, Alan R. Liss, Inc., 150 Fifth Avenue, New York, NY10011, 1983, p.365−377.
- Inoe H., Inagaki K., Sugimoto M., Esaki N., Soda K. & Tanaka H. Structural analysis of the L-methionine gamma-lyase gene from Pseudomonas putida. //J.Biochem., 1995, v. 117, p. 1120−1125.
- Goodal G., Mottram J.C., Coombs G.H., and Laptom A.J. PDB-Entry 1E5E, 2000.
- Bazhulina N.P., Morozov Yu.V., Papisova A.I., Demidkina T.V. Pyridoxal 5'-phosphate Schiff base in Citrobacter freundii tyrosine phenol-lyase: ionic and tautomeric equilibria. // EJB, 2000, v. 267, p. 1830−1836.
- Bazhulina N.P., Bokovoi V.A., Morozov Yu.V., Fiodorova L.I. & Chekhov V.O. Spectroscopic behavior of pyridoxal 5'-phosphate amino acid aldimines. Tautomer and isomer equilibria. //Molekulyarnaya Biologiya (in Russian), 1991, v. 25, p. 546−555.
- Metzler C.M., Viswanath R. & Metzler D.E. Equilibria and absorption spectra of tryptophanase. //J. Biol. Chem., 1991, v. 266, p. 9374−9381.
- Ph. & Metzler D.E., eds), Wiley-Interscience, NY, USA, 1985, p. 37 108.
- Aitken S.M., and Kirsch J.F. Kinetics of the yeast cystathionine beta-synthase forward and reverse reactions: continuous assays and the equilibrium constant for the reaction. 11 Biochemistry, 2003, v. 42, p. 571−578.
- A itken S.M., Kim D.H., and Kirsch J.F. Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactions. //Biochemistry, 2003, v. 42, p. 11 297−11 306.
- Cook P.F., and Cleland W.W. pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same. //Biochemitry, 1981, v. 20, p. 1797−1805.
- Sambrook J., Fritsch E.F.& Maniatis T. Molecular Cloning: A Laboratory Manual. Second Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1989.
- Sanger F., Nicklen S. & Coulsen A.R. DNA sequencing with chain-terminating inhibitors. UProc. Natl. Acad. Sci. USA., 1977, v. 74, p. 5463−5467.
- Π Π°ΡΡΠΎΡΠ³ΡΠ΅Π² C.M., ΠΠ°Π²ΠΈΠ»ΡΠ³Π΅Π»ΡΡΠΊΠΈΠΉ Π. Π. //ΠΠ΅Π½Π΅ΡΠΈΠΊΠ°, 2003, Ρ. 39, Ρ. 218−224.
- Fridemann Π’.Π., Haugen G.E. The determination of keto acids in blood and urine. IIJ. Biol. Chem., 1943, v. 177(2), p. 415−442.
- Π€ΡΡΡΡ Π. Π‘ΡΡΡΠΊΡΡΡΠ° ΠΈ ΠΌΠ΅Ρ Π°Π½ΠΈΠ·ΠΌ Π΄Π΅ΠΉΡΡΠ²ΠΈΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠΎΠ². Π., ΠΠΈΡ, 1980.
- Cleland W. Statistical analysis of enzyme kinetic data. //Methods Enzymol., 1979, v. 63, p. 103−138.
- Lowry O.H., Rosenbrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. IIJ. Biol. Chem., 1951, v. 193, p. 265−275.
- Peterson E.A., Sober H.A. Preparation of crystalline phosphorylated derivatives of Vitamin B6. HJ. Amer. Chem. Soc., 1954, v. 76, p 169−175.
- Metzler D.E., Harris C.M., Johnson R.J. & Siano D.B. Spectra of 3-hydroxypyridines. Band-shape analysis and evaluation of tautomeric equilibria. //Biochemistry, 1973, v. 12, p. 5377−5392.
- Glasoe P.V., Long F.A. //J. Phys. Chem. 1960, v. 64, p. 188−194.
- Manukhov I.V., Demidkina T.V., Mamaeva D.V., Rastorguev S.M. and Zavilgelsky G.B. Citrobacter freundii methionine y-lyase (megL) and putative amino acid permease (aap) genes, complete cds, 2003, Gene bank accession number: AY204910.
- Mamaeva D.V., Morozova E.A., Nikulin A.D., Revtovich S.V., Nikonov S.V., Garber M.B., Demidkina T.V. Structure of Citrobacter freundii L-methionine y-lyase. Acta Cryst., 2005, F61, p. 546−549.
- ΠΠ°Π½ΡΡ ΠΎΠ² Π.Π., ΠΠ°ΠΌΠ°Π΅Π²Π° Π. Π., ΠΠΎΡΠΎΠ·ΠΎΠ²Π° Π. Π., Π Π°ΡΡΠΎΡΠ³ΡΠ΅Π² Π‘. Π., Π€Π°Π»Π΅Π΅Π² Π. Π., ΠΠ΅ΠΌΠΈΠ΄ΠΊΠΈΠ½Π° Π’. Π. ΠΠ°Π²ΠΈΠ»ΡΠ³Π΅Π»ΡΡΠΊΠΈΠΉ Π.Π. L-ΠΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ Ρ-Π»ΠΈΠ°Π·Π° Citrobacter freundii'. ΠΊΠ»ΠΎΠ½ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ Π³Π΅Π½Π° ΠΈ ΠΊΠΈΠ½Π΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΡ ΡΠ΅ΡΠΌΠ΅Π½ΡΠ°. ΠΠΈΠΎΡ ΠΈΠΌΠΈΡ (ΠΠΎΡΠΊΠ²Π°), 2006, Ρ. 71(4), Ρ. 454 463.
- Revtovich S.V., Mamaeva D.V., Morozova Π.Π., Nikulin A.D., Nikonov S.V., Garber M.B., Demidkina T.V. Crystal Sructure of Citrobacter freundii L-methionine y-lyase, 2004, PDB: 1Y4I.
- ΠΠ°ΡΠ΅ΡΠΈΠ°Π»Ρ ΡΠ°Π±ΠΎΡΡ, ΠΎΠΏΡΠ±Π»ΠΈΠΊΠΎΠ²Π°Π½Π½ΡΠ΅ Π² Π²ΠΈΠ΄Π΅ ΡΠ΅Π·ΠΈΡΠΎΠ² ΡΠΎΠΎΠ±ΡΠ΅Π½ΠΈΠΉΠ½Π° ΠΊΠΎΠ½ΡΠ΅ΡΠ΅Π½ΡΠΈΡΡ
- ΠΠ°ΠΌΠ°Π΅Π²Π° Π.Π., ΠΠ°ΡΠ±ΠΎΠ»ΠΈΠ½Π° Π. Π., ΠΠ΅ΠΌΠΈΠ΄ΠΊΠΈΠ½Π° Π’.Π. L-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ Ρ-Π»ΠΈΠ°Π·Π° Citrobacter freundii-. ΠΌΠ΅ΡΠΎΠ΄ ΠΎΡΠΈΡΡΠΊΠΈ ΠΈ Π½Π΅ΠΊΠΎΡΠΎΡΡΠ΅ ΡΠ²ΠΎΠΉΡΡΠ²Π°. Π’Π΅Π·ΠΈΡΡ ΡΠΊΠΎΠ»Ρ-ΠΊΠΎΠ½ΡΠ΅ΡΠ΅Π½ΡΠΈΠΈ «ΠΠΎΡΠΈΠ·ΠΎΠ½ΡΡ ΡΠΈΠ·ΠΈΠΊΠΎ-Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΎΠΉ Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΠΈ», ΠΡΡΠΈΠ½ΠΎ, Π ΠΎΡΡΠΈΡ, 2000, Ρ.2, Ρ. 250.
- Mamaeva D.V., Faleev N.G., Demidkina T.V. Purification and some properties of L-methionine y-lyase from Citrobacter freundii. The 5-th International Engelhardt Conference on molecular biology. June 2126, 2001, Moscow (Russia), posters session.
- ΠΠ°ΠΌΠ°Π΅Π²Π° Π.Π., Π€Π°Π»Π΅Π΅Π² Π. Π., ΠΠ΅ΠΌΠΈΠ΄ΠΊΠΈΠ½Π° Π’. Π. ΠΡΠ΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΈ ΡΠ²ΠΎΠΉΡΡΠ²Π° L-ΠΌΠ΅ΡΠΈΠΎΠ½ΠΈΠ½ — Ρ-Π»ΠΈΠ°Π·Ρ ΠΈΠ· Citrobacter freundii. Ill ΡΡΠ΅Π·Π΄ Π±ΠΈΠΎΡ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΎΠ±ΡΠ΅ΡΡΠ²Π° Π ΠΠ. Π’Π΅Π·ΠΈΡΡ Π½Π°ΡΡΠ½ΡΡ Π΄ΠΎΠΊΠ»Π°Π΄ΠΎΠ², Ρ. 592, 26 ΠΈΡΠ½Ρ — 1 ΠΈΡΠ»Ρ 2002, Π‘Π°Π½ΠΊΡ-ΠΠ΅ΡΠ΅ΡΠ±ΡΡΠ³, Π ΠΎΡΡΠΈΡ.
- Manukhov I.V., Rastorguev S.M., Zavilgelsky G.B., Mamaeva D.V., Demidkina T.V. Gene cloning and characterization of Citrobacter freundii L-methionine y-lyase. 1st Congress of European of
- Microbiologists. Poster session. Slovenia, Ljubljana, Cankarjevdom, June 29 July 3, 2003. ΠΊ