ACID PROTEASE IN NEPENTHES .2. STUDY ON SPECIFICITY OF NEPENTHESIN

被引：24

作者：

AMAGASE, S

NAKAYAMA, S

TSUGITA, A

机构：

[1] Faculty of the Science of Living, Osaka City University, Osaka

[2] Laboratory of Molecular Genetics, Medical School, University of Osaka, Osaka

来源：

JOURNAL OF BIOCHEMISTRY | 1969年 / 66卷 / 04期

关键词：

D O I：

10.1093/oxfordjournals.jbchem.a129166

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：

The substrate specificity of the partially purified acid protease in Nepenthes (nepenthesin) was studied by hydrolyzing several peptides of known structures. The results indicated that nepenthesin was predominantly specific to aspartic acid residue at its carboxyl side or at its amino side, and was apparently specific also to tyrosine and alanine residues at their carboxyl sides. The protease seemed to be an endopeptidase. © 1969 BY THE JOURNAL OF BIOCHEMISTRY.

引用

页码：431 / &

共 12 条

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