PYRROLIDONECARBOXYLYL PEPTIDASE - STABILIZATION AND PURIFICATION

被引:43
作者
ARMENTROUT, RW
DOOLITTLE, RF
机构
[1] Departments of Biology and Chemistry, University of California, La Jolla
基金
美国国家卫生研究院;
关键词
D O I
10.1016/0003-9861(69)90339-7
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
Pyrrolidonecarboxylyl peptidase, an enzyme which specifically hydrolyzes aminoterminal pyrrolidonecarboxylyl residues from peptides, has been stabilized and purified. The enzymatic activity, derived from a strain of Pseudomonas fluorescens, was protected during purification by the addition of 2-pyrrolidone to all solutions. The final preparation exhibited two close bands on acrylamide gel and was 200 times more active than the crude material. The enzyme demonstrated the ability to specifically remove pyrrolidonecarboxylyl groups from a high molecular weight protein. © 1969.
引用
收藏
页码:80 / +
页数:1
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