The activating system of chitin synthetase from Saccharomyces cerevisiae. Purification and properties of an inhibitor of the activating factor.
The activating system of chitin synthetase from Saccharomyces cerevisiae. Purification and properties of an inhibitor of the activating factor.
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酿酒酵母几丁质合成酶的激活系统。
DOI：
10.1016/s0021-9258(19)42588-x
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发表时间：
1974
期刊：
影响因子：
--
通讯作者：
E. Cabib
中科院分区：
文献类型：
--
作者：
R. Ulane;E. Cabib
从酿酒酵母中分离纯化了激活几丁质合成酶酶原的酵母蛋白酶抑制剂。通过圆盘凝胶电泳和凝胶电聚焦，蛋白质似乎是均一的。在6 mguanidine盐酸盐存在下通过凝胶过滤测定的抑制剂的分子量估计为约8500，没有亚基存在的证据。氨基酸分析显示不存在半胱氨酸、甲硫氨酸、精氨酸和色氨酸。NH 2-末端残基是苏氨酸。对S.卡尔氏酵母和卡尔氏酵母揭示了这两种蛋白质具有相同的分子大小，但在电荷上有很大的不同。
The protein inhibitor of the yeast protease which activates chitin synthetase zymogen has been purified fromSaccharomyces cerevisiae. The protein appears to be homogeneous by disc gel electrophoresis and gel electrofocusing. The molecular weight of the inhibitor, as determined by gel filtration in the presence of 6mguanidine hydrochloride, is estimated to be about 8500, with no evidence for the existence of subunits. Amino acid analysis shows the absence of cysteine, methionine, arginine, and tryptophan. The NH2-terminal residue is threonine. Comparison of the inhibitors fromS. cerevisiaeandSaccharomyces carlsbergensisrevealed that both proteins are of equivalent molecular size but differ substantially in electrical charge.