Cleavage of BSA by a dipeptide seryl-histidine

被引：17

作者：

Chen, J ^{[1
]}

Wan, R ^{[1
]}

Liu, H ^{[1
]}

Cheng, CM ^{[1
]}

Zhao, YF ^{[1
]}

机构：

[1] Tsinghua Univ, Dept Chem, Sch Life Sci & Engn, Educ Minist,Key Lab Bioorgan Phosphorus Chem, Beijing 100084, Peoples R China

来源：

LETTERS IN PEPTIDE SCIENCE | 2000年 / 7卷 / 06期

关键词：

artificial enzyme; bovine serum albumin; chemical protease; protein cleavage; seryl-histidine;

D O I：

10.1007/BF02443596

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

A dipeptide seryl-histidine (Ser-His) was found to have the protein cleavage activity. BSA was cleaved into smear at around pH 5.0-6.0, with a half-life around 15 hr at 60 degreesC. Phosphate could accelerate the reaction. This is a brand new protein cleavage system. Since Ser and His are well-known catalytic residues at the active sites of many serine proteases, this results might provide clues to the possible roles of short oligopeptides in the origins of modem enzymes.

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收藏

页码：325 / 329

页数：5

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