IDENTIFICATION OF THE 38-KDA SUBUNIT OF RABBIT SKELETAL-MUSCLE GLYCOGEN-SYNTHASE AS GLYCOGENIN
IDENTIFICATION OF THE 38-KDA SUBUNIT OF RABBIT SKELETAL-MUSCLE GLYCOGEN-SYNTHASE AS GLYCOGENIN
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DOI：
10.1111/j.1432-1033.1987.tb13637.x
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发表时间：
1987-12-15
期刊：
影响因子：
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通讯作者：
COHEN, P
中科院分区：
文献类型：
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作者：
PITCHER, J;SMYTHE, C;COHEN, P
兔骨骼肌糖原合成酶已被证明是两种亚基的复合体，其表观分子质量为86 kDa和38 kDa，摩尔比为1:1。在2 M LiBr的存在下，通过凝胶过滤将38-kDa组分从86-kDa催化亚基中分离出来，并对许多胰凝肽进行了测序。这表明38-kDa亚基是糖原，一种与糖原共价结合的蛋白质，被认为是参与从头合成糖原起始的“引物”。
Glycogen synthase from rabbit skeletal muscle has been shown to be a complex of two types of subunit which have apparent molecular masses of 86 kDa and 38 kDa and are present in a 1:1 molar ratio. The 38-kDa component was separated from the 86-kDa catalytic subunit by gel filtration in the presence of 2 M LiBr, and a number of chymotryptic peptides were sequenced. This demonstrated that the 38-kDa subunit was glycogenin, the protein that is bound covalently to glycogen and believed to be the ''primer'' involved in the initiation of de novo glycogen synthesis.