PURIFICATION AND SOME PROPERTIES OF MEMBRANE-BOUND AND SOLUBLE PYROPHOSPHATASES OF YEAST VACUOLES

被引：18

作者：

LICHKO, L

OKOROKOV, L

机构：

[1] Institute of Biochemistry and Physiology of Microorganisms, U.S.S.R. Academy of Sciences, Puschino

来源：

YEAST | 1991年 / 7卷 / 08期

关键词：

YEAST; VACUOLES; PYROPHOSPHATASE; H+-TRANSPORT;

D O I：

10.1002/yea.320070805

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 membrane-bound and soluble pyrophosphatase (PPase) activities of Saccharomyces carlsbergensis vacuoles are determined by the functioning of special enzymes and are not due to non-specific PP(i) hydrolysis by other vacuolar phosphohydrolases. The molecular mass of the membrane-bound PPase is apparently 120 000 and its molecule consists of three subunits with M(r) = 41 000. Soluble PPase has a molecular mass of about 82 000 and includes three subunits with M(r) = 28 000. Both enzymes are glycoproteins. The vacuolar membrane-bound PPase is a proton pump.

引用

页码：805 / 812

页数：8

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