面包酵母转酮醇酶分子中的亚基间二硫键。
Intersubunit disulfide bonds in the molecule of baker's yeast transketolase.
作者信息
Solovjeva O N, Kochetov G A
机构信息
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.
出版信息
Biochem Mol Biol Int. 1994 Nov;34(5):1049-54.
PMID:7703900
Abstract
It has previously been shown that baker's yeast trans ketolase has no intersubunit disulfide bonds and is able to dissociate reversibly into subunits at a low apoprotein concentration in solution. By contrast, in the present work it was found that in the molecule of transketolase C (a newly discovered form of the enzyme) subunits are bound to each other by disulfide bonds.
摘要
先前的研究表明，面包酵母转酮醇酶没有亚基间二硫键，并且在溶液中低脱辅基蛋白浓度下能够可逆地解离成亚基。相比之下，在目前的研究中发现，在转酮醇酶C（该酶的一种新发现形式）分子中，亚基通过二硫键相互结合。
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