Purification, characterization and partial amino acid sequence of glycogen synthase from Saccharomyces cerevisiae.
Purification, characterization and partial amino acid sequence of glycogen synthase from Saccharomyces cerevisiae.
复制标题
酿酒酵母糖原合酶的纯化、表征和部分氨基酸序列。
DOI：
10.1042/bj2680401
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发表时间：
1990
期刊：
影响因子：
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通讯作者：
J. Guinovart
中科院分区：
文献类型：
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作者：
A. Carabaza;J. Ariño;J. Fox;C. Villar;J. Guinovart
从酿酒酵母中纯化糖原合成酶达到均匀性。酶的亚基分子质量为80 kDa。全酶似乎是一个四聚体。针对纯化酵母糖原合成酶的抗体使酵母提取物中的酶失活，并允许在Western blots中检测蛋白质。氨基酸分析表明该酶含有丰富的谷氨酸和/或谷氨酰胺残基。测定了n端序列（11个氨基酸残基）。此外，选定的胰蛋白酶消化肽通过反相高效液相色谱纯化，并提交气相测序。多达8个序列（79个氨基酸残基）可以与人类肌肉酶序列对齐。同源水平在37%到100%之间，这表明，尽管人类和酵母糖原合成酶可能共享一些保守区域，但它们的初级结构应该存在显著差异。
Glycogen synthase from Saccharomyces cerevisiae was purified to homogeneity. The enzyme showed a subunit molecular mass of 80 kDa. The holoenzyme appears to be a tetramer. Antibodies developed against purified yeast glycogen synthase inactivated the enzyme in yeast extracts and allowed the detection of the protein in Western blots. Amino acid analysis showed that the enzyme is very rich in glutamate and/or glutamine residues. The N-terminal sequence (11 amino acid residues) was determined. In addition, selected tryptic-digest peptides were purified by reverse-phase h.p.l.c. and submitted to gas-phase sequencing. Up to eight sequences (79 amino acid residues) could be aligned with the human muscle enzyme sequence. Levels of identity range between 37 and 100%, indicating that, although human and yeast glycogen synthases probably share some conserved regions, significant differences in their primary structure should be expected.