Human brain calmodulin: isolation, characterization, and sequence of a half-molecule fragment.
Human brain calmodulin: isolation, characterization, and sequence of a half-molecule fragment.
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人脑钙调蛋白：半分子片段的分离、表征和序列。
DOI：
10.1021/bi00521a022
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Fischer,EH
中科院分区：
文献类型：
--
作者：
Schreiber,WE;Sasagawa,T;Titani,K;Wade,RD;Malencik,D;Fischer,EH
William E.Schreiber，*Tatsuru Sasagawa，Koiti Titani，8 Roger D.Wade，Dean Malencik，*和Edmond H.Fischer*摘要：从人脑中纯化出一种钙结合蛋白，并鉴定为钙调蛋白的72-148个残基。该半分子片段(CaM72_I48)含有钙调蛋白15个碱性氨基酸中的11个(包括1个三甲基赖氨酸)，并显示出较高的等电点。酪氨酸和八个苯丙氨酸残基中的三个也存在于片段中，导致吸收光谱略有不同。虽然CaM72_148含有两个钙调蛋白的钙结合部位，但每个分子只结合一个钙离子
William E. Schreiber,* Tatsuru Sasagawa, Koiti Titani, 8 Roger D. Wade, Dean Malencik,* and Edmond H. Fischer* abstract: A Ca2+-binding protein from human brain has been purified to homogeneityand identified as residues 72-148 of calmodulin. This half-molecule fragment (CaM72_i48) contains 11 of calmodulin’s 15 basic amino acids (including one trimethyllysine) and demonstrates a higher isoelectric point. Both tyrosines and three of eight phenylalanine residues also occur in the fragment, giving rise to a somewhat different absorption spectrum. Though it contains two of calmodulin’s Ca2+-binding sites, CaM72_148 binds only one Ca2+ per molecule