PURIFICATION AND SOME PROPERTIES OF 2 PROTEASES FROM PAPAYA LATEX

被引：39

作者：

LYNN, KR

机构：

[1] Division of Biological Sciences, National Research Council of Canada, Ottawa

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 569卷 / 02期

关键词：

(Papaya); Latex; Protease;

D O I：

10.1016/0005-2744(79)90054-8

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：

Two proteases, one of which is papaya peptidase A and the other a previously unknown enzyme in papaya latex have been purified to homogeneity in a simple two stage process. Both are markedly less reactive than papain or chymopapain. Each has a molecular weight of 24 000, N-terminal sequences commencing Leu-Pro-Glu, and contains no carbohydrate. Their amino acid compositions differ for several residues. The essential -SH groups of the enzymes examined appear to be 'masked' in the native state. © 1979.

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收藏

页码：193 / 201

页数：9

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