Comparison of calcium-modulated proteins from vertebrate brains.
Comparison of calcium-modulated proteins from vertebrate brains.
复制标题
脊椎动物大脑中钙调节蛋白的比较。
DOI：
10.1021/bi00553a020
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发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
T. Vanaman
中科院分区：
文献类型：
--
作者：
D. M. Watterson;D. M. Watterson;P. A. Mendel;P. A. Mendel;T. Vanaman
已经从猪脑、兔脑、大鼠脑和鸡脑中纯化了钙调素，并将它们的结构和功能特性与牛脑蛋白质的结构和功能特性进行了比较，牛脑蛋白质的完整氨基酸序列已经阐明。这五种蛋白质的氨基酸组成和胰蛋白酶肽图没有重大差异。所有钙调素缺乏色氨酸和半胱氨酸，每摩尔蛋白质含有1摩尔N ε-三甲基赖氨酸和组氨酸。牛、猪、兔、大鼠和鸡脑钙调素在聚丙烯酰胺凝胶上共迁移，在存在和不存在变性剂的各种条件下运行。所有的脑钙调素给出了相同的配置文件的钙依赖性激活的“可激活的”牛脑3 '，5'-环核苷酸磷酸二酯酶。此外，它们与兔骨骼肌肌钙蛋白I形成钙依赖性复合物，且复合物的电泳迁移率彼此相同，与肌钙蛋白I和肌钙蛋白C之间的相应复合物相似。这些研究更全面地定义了什么是钙调素，证明了钙调素是脊椎动物脑中相对不变的成分，并表明钙调素的结构和功能在脊椎动物进化过程中高度保守。
Calmodulins have been purified from porcine, rabbit, rat, and chicken brains and their structural and functional properties compared to those of the bovine brain protein whose complete amino acid sequence has been elucidated. No major differences were detected in the amino acid compositions and tryptic peptide maps of these five proteins. All calmodulins lacked tryptophan and cysteine and contained 1 mol of N epsilon-trimethyllysine and histidine per mol of protein. Bovine, porcine, rabbit, rat, and chicken brain calmodulins comigrated on polyacrylamide gels run under a variety of conditions in the presence and absence of denaturants. All brain calmodulins gave identical profiles for the calcium-dependent activation of "activatable" bovine brain 3',5'-cyclic nucleotide phosphodiesterase. In addition, they formed calcium-dependent complexes with rabbit skeletal muscle troponin I and the electrophoretic mobilities of the complexes were identical with one another and similar to the corresponding complex between troponin I and troponin C. These studies more fully define what is a calmodulin, demonstrate that calmodulin is a relatively invariant constituent of vertebrate brain, and indicate that calmodulin structure and function have been highly conserved throughout vertebrate evolution.