牛和羊κ-酪蛋白构象的预测。
Prediction of the conformation of the cow and sheep kappa-caseins.
作者信息
Loucheux-Lefebvre M H, Aubert J P, Jollès P
出版信息
Biophys J. 1978 Sep;23(3):323-36. doi: 10.1016/S0006-3495(78)85452-6.
Abstract
The secondary structures of cow and sheep kappa-caseins were established according to the predictive rules of Chou and Fasman. The diagrams derived from this treatment allowed us to study the chymosin sensitive bond (milk-clotting process), as well as the glycosylation and phosphorylation sites, found to be situated in beta-turns. Despite a high variability between the primary structures of the COOH-terminal part (caseinoglycopeptide) of cow, sheep, and also other caseins, the secondary structures of the biologically important sites were found to be conserved.
摘要
根据Chou和Fasman的预测规则确定了牛和羊κ-酪蛋白的二级结构。从该处理得出的图表使我们能够研究凝乳酶敏感键（凝乳过程）以及糖基化和磷酸化位点，发现它们位于β-转角处。尽管牛、羊以及其他酪蛋白的COOH末端部分（酪蛋白糖肽）的一级结构存在很大差异，但发现生物学重要位点的二级结构是保守的。
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本文引用的文献
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Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
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CASEINO-GLYCOPEPTIDES: CHARACTERIZATION OF A METHIONINE RESIDUE AND OF THE N-TERMINAL SEQUENCE.酪蛋白糖肽：甲硫氨酸残基及N端序列的表征
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[Comparative study of the caseinoglycopeptides formed by the action of rennin on caseins from the cow, sheep and goat. II. Study of the non-peptide portion].[凝乳酶作用于牛、羊和山羊酪蛋白形成的酪蛋白糖肽的比较研究。II. 非肽部分的研究]
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