Peptide synthesis catalyzed by subtilisin-72 in organic solvents [Peptidnyi sintez, kataliziruemyi subtilizinom-72 v organicheskikh rastvoriteliakh.]

Авторы: Getun I.V., Filippova I.I., Lysogorskaia E.N., Bacheva A.V., Oksenoǐt E.S.
Журнал: Bioorganicheskaia khimiia
Том: 25
Номер: 8
Год издания: 1999
Первая страница: 591
Последняя страница: 596
Аннотация: http://www.ncbi.nlm.nih.gov/pubmed/10578464 http://www.rjbc.ru/arc/25/8/0591-0596.pdf The solubility, stability, and activity of native subtilisin 72 and of its complex with SDS were comparatively studied in a number of polar organic solvents. Subtilisin was found to catalyze peptide bond formation when suspended in acetonitrile or solubilized as a complex with SDS in ethanol and isopropanol. Tripeptide Z-Ala-Ala-Leu-pNA, tetrapeptides A-Ala-Ala-P1-P1'-B, where A = Z or Abz; P1 = Leu, Phe, Met, Trp, Ile, Tyr, Phe(NO2), or Glu(OMe), P1' = Leu, Phe, Glu, Ala, Ile, Val, or Arg; B = NH2, pNA, or 2-(2,4-dinitrophenyl)aminoethylamine residue (Ded); pentapeptides Z-Ala-Ala-Leu-Ala-Ala-pNA and Z-Ala-Ala-Leu-Ala-Phe-pNA; and hexapeptide Abz-Val-Ala-Phe-Phe-Ala-Ala-Ded were synthesized using the SDS-subtilisin complex. The complex also efficiently catalyzed the oligomerization of tripeptide H-Phe-Ala-Leu-OCH3 in ethanol, which resulted in a 63:37 mixture of trioligomer and tetraoligomer. It was demonstrated that SDS-subtilisin is a much more efficient catalyst than the suspension of native enzyme.
Добавил в систему: Бачева Анна Владимировна

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