Toda H, Yazawa M, Yagi K
Institute for Protein Research, Osaka University, Japan.
Eur J Biochem. 1992 Apr 15;205(2):653-60. doi: 10.1111/j.1432-1033.1992.tb16824.x.
The complete amino acid sequence of calmodulin from Euglena gracilis was determined by isolation and sequence analyses of peptides derived from calmodulin by digestion with trypsin and Staphylococcus aureus V8 protease. Euglena calmodulin consists of 148 amino acid residues; it lacks tryptophan and cysteine and contains one tyrosine, three histidine and two NE-trimethyllysine residues/molecule of the protein. Its N-terminus was blocked with an acetyl group and C-terminal lysine was trimethylated. Euglena calmodulin is the first calmodulin so far examined in which the C-terminal lysine is trimethylated. The comparison of amino acid sequences between Euglena and human brain calmodulins indicated 17 amino acid substitutions in Euglena calmodulin.
通过对经胰蛋白酶和金黄色葡萄球菌V8蛋白酶消化后从钙调蛋白衍生的肽段进行分离和序列分析，确定了纤细裸藻钙调蛋白的完整氨基酸序列。纤细裸藻钙调蛋白由148个氨基酸残基组成；它不含色氨酸和半胱氨酸，每分子蛋白质含有一个酪氨酸、三个组氨酸和两个Nε-三甲基赖氨酸残基。其N端被乙酰基封闭，C端赖氨酸被三甲基化。纤细裸藻钙调蛋白是迄今为止检测到的第一个C端赖氨酸被三甲基化的钙调蛋白。纤细裸藻和人脑钙调蛋白氨基酸序列的比较表明，纤细裸藻钙调蛋白中有17个氨基酸替换。
