LIMITED PROTEOLYSIS OF CYTOCHROME-C IN TRIFLUOROETHANOL

被引：34

作者：

FONTANA, A

ZAMBONIN, M

DEFILIPPIS, V

BOSCO, M

DELAURETO, PP

机构：

[1] CRIBI Biotechnology Centre, University of Padua, 35121 Padua

来源：

FEBS LETTERS | 1995年 / 362卷 / 03期

关键词：

CYTOCHROME C; LIMITED PROTEOLYSIS; PROTEIN FRAGMENT; TRIFLUOROETHANOL; CIRCULAR DICHROISM;

D O I：

10.1016/0014-5793(95)00237-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Horse heart cytochrome c is cleaved by thermolysin in 50% aqueous TFE (v/v) at neutral pH (25 degrees C, 24 h) at the Gly(56)-Ile(57) peptide bond of the 104-residue chain of the protein. Additional, but anyway minor, fragmentation at the Gly(45)-Phe(46) and Met(80)-Ile(81) peptide bonds is also observed. On the other hand, in buffer only and in the absence of TFE, cytochrome c is digested by thermolysin to numerous small peptides. Considering the broad substrate specificity of the TFE-resistant thermolysin, clearly the conformational state of the protein substrate dictates the observed selective proteolysis. It is proposed that the highly helical secondary structure acquired by cytochrome c when dissolved in aqueous TFE hampers binding and adaptation of the protein substrate at the active site of the protease and that peptide bond fission occurs at flexible chain segments characterized by a low alpha-helix propensity.

引用

页码：266 / 270

页数：5

共 38 条

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