Determination of the complete amino acid sequence of bovine cardiac troponin C.
Determination of the complete amino acid sequence of bovine cardiac troponin C.
复制标题
牛心肌肌钙蛋白C完整氨基酸序列的测定。
DOI：
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发表时间：
1976
期刊：
影响因子：
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通讯作者：
Kenji Takahashi
中科院分区：
文献类型：
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作者：
J. P. Eerd;Kenji Takahashi
牛心肌肌钙蛋白C的氨基酸序列已完全测定。用溴化氰裂解蛋白质，分离得到的肽。该蛋白质的161个残基全部可以用12个溴化氰肽来解释。通过胰蛋白酶消化柠康酰化肌钙蛋白C并分离所得五种肽产生重叠肽。心肌肌钙蛋白C的一级结构通过这些肽的连续手动Edman降解来阐明。它由四个同源区域组成，其中一个可能已经失去了结合钙离子的能力。通过比较心肌肌钙蛋白C的氨基酸序列与骨骼肌肌钙蛋白C的序列，发现不结合钙的区域的突变率几乎是结合钙的三个同源区域的突变率的两倍。
: The amino acid sequence of bovine cardiac troponin C has been completely determined. The protein was cleaved by cyanogen bromide and the resulting peptides were isolated. All of the 161 residues of the protein could be accounted for in 12 cyanogen bromide peptides. Overlapping peptides were generated by tryptic digestion of citraconylated troponin C and isolation of the resulting five peptides. The primary structure of cardiac troponin C was elucidated by sequential manual Edman degradation of these peptides. It consists of four homologous regions, one of which probably has lost the ability to bind calcium ions. By comparing the amino acid sequence of cardiac troponin C with the sequence of skeletal troponin C, it was found that the mutation rate of the region that does not bind calcium is almost twice as high as the mutation rate of the three homologous regions that do bind calcium.