Wilkinson J M
Eur J Biochem. 1980 Jan;103(1):179-88. doi: 10.1111/j.1432-1033.1980.tb04302.x.
Troponin C has been isolated from rabbit slow skeletal and cardiac muscle and the complete amino acid sequence of the slow muscle protein determined. Amino acid analysis and peptide mapping of the cardiac protein showed it to be very similar to, if not identical with, the slow muscle protein. This identity has been proved by the isolation and characterisation of tryptic peptides from the cardiac protein. It seems very likely that troponin C from these two tissues is the product of a single gene, in contrast to troponin I and troponin T which are the products of different genes. The amino acid sequences shows only one difference from that of bovine cardiac troponin C, the highly conservative replacement of an aspartic for a glutamic acid at position 115. No differences were found in the N-terminal region where these proteins appear to have a lost one of the Ca2+ binding sites found in fast skeletal muscle troponin C. The possible significance of this finding in relation to the binding of troponin C to the different types of troponin I is discussed.
肌钙蛋白C已从兔慢肌骨骼肌和心肌中分离出来，并且测定了慢肌蛋白的完整氨基酸序列。对心肌蛋白的氨基酸分析和肽图谱分析表明，它即便与慢肌蛋白不完全相同，也非常相似。从心肌蛋白中分离并鉴定胰蛋白酶肽段已证明了这种一致性。与肌钙蛋白I和肌钙蛋白T是不同基因的产物相反，这两种组织的肌钙蛋白C似乎很可能是单个基因的产物。该氨基酸序列与牛心肌肌钙蛋白C的序列仅显示出一处差异，即在第115位高度保守地将天冬氨酸替换为谷氨酸。在N端区域未发现差异，在该区域这些蛋白似乎已经失去了快速骨骼肌肌钙蛋白C中发现的一个Ca2+结合位点。讨论了这一发现与肌钙蛋白C与不同类型肌钙蛋白I结合的可能意义。
