枯草杆菌素
盐(化学)
化学
基质(水族馆)
氨基酸
离子强度
盐析
生物物理学
生物化学
酶
有机化学
生物
生态学
水溶液
作者
Hanne Grøn,Lene M. Bech,Klaus Breddam
出处
期刊:Protein and Peptide Letters
[Bentham Science]
日期:1994-09-01
卷期号:1 (2): 106-113
标识
DOI:10.2174/0929866501666220424134356
摘要
The proteolytic activity of the subtilisin Savinase is, with some substrates, radically enhanced at increased ionic strength. At some substrate positions the incorporation of more hydrophobic amino acid residues enhances the beneficial effects of salt addition. At other positions only the incorporation of charged amino acid residues leads to a significant change in the salt dependency. When the substrates are optimized with respect to hydrophobic interactions the enhancing effect of salt. declines. This demonstrates that the beneficial (rate enhancing) effects of salt addition cannot always be accounted for by simple models, e.g., the traditional "salting out" model.
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