酵母液泡膜结合型和可溶性焦磷酸酶的纯化及某些特性
Purification and some properties of membrane-bound and soluble pyrophosphatases of yeast vacuoles.
作者信息
Lichko L, Okorokov L
机构信息
Institute of Biochemistry and Physiology of Microorganisms, U.S.S.R. Academy of Sciences, Puschino, Moscow Region.
出版信息
Yeast. 1991 Nov;7(8):805-12. doi: 10.1002/yea.320070805.
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 PPi 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 Mr = 41,000. Soluble PPase has a molecular mass of about 82,000 and includes three subunits with Mr = 28,000. Both enzymes are glycoproteins. The vacuolar membrane-bound PPase is a proton pump.
卡尔斯伯酵母液泡的膜结合型和可溶性焦磷酸酶（PPase）活性由特殊酶的功能决定，并非其他液泡磷酸水解酶的非特异性焦磷酸（PPi）水解所致。膜结合型PPase的分子量显然为120,000，其分子由三个Mr = 41,000的亚基组成。可溶性PPase的分子量约为82,000，包含三个Mr = 28,000的亚基。这两种酶都是糖蛋白。液泡膜结合型PPase是一种质子泵。
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