Biochemical properties of Bacillus intermedius subtilisin-like proteinase secreted by a Bacillus subtilis recombinant strain in its stationary phase of growth

被引：12

作者：

Mikhailova, E. O. ^{[1
]}

Mardanova, A. M. ^{[1
]}

Balaban, N. P. ^{[1
]}

Rudenskaya, G. N. ^{[2
]}

Ilyinskaya, O. N. ^{[1
]}

Sharipova, M. R. ^{[1
]}

机构：

[1] Kazan VI Lenin State Univ, Kazan 420008, Russia

[2] Moscow MV Lomonosov State Univ, Fac Chem, Moscow 119992, Russia

来源：

BIOCHEMISTRY-MOSCOW | 2009年 / 74卷 / 03期

基金：

俄罗斯基础研究基金会;

关键词：

subtilisin-like proteinase; AprBi; dimers; INTRACELLULAR SERINE PROTEASE; AMYLOLIQUEFACIENS SUBTILISIN; CLONING; LICHENIFORMIS; SPORULATION; EXPRESSION; ENZYMES; CELLS; GENE;

D O I：

10.1134/S0006297909030109

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：

Biochemical properties of Bacillus intermedius subtilisin-like proteinase (AprBi) secreted by a B. subtilis recombinant strain in the early and late stationary phases of growth have been determined. Protein structure was analyzed and its stability estimated. It was noted that the enzyme corresponding to different phases of bacterial growth retains activity in the presence of reducing and oxidizing agents (C2H5OH and H2O2). Different effects of bivalent metal ions on activity of two proteinase fractions were found. Calcium ions more efficiently activate proteinase secreted in the late stationary phase. Unlike the first enzyme fraction, the second forms catalytically active dimers.

引用

页码：308 / 315

页数：8

共 36 条

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