Shiraishi F
Department of Clinical Pharmacology, Faculty of Medicine, Kyushu University 60, Fukuoka.
Fukuoka Igaku Zasshi. 1993 Jul;84(7):339-44.
The Ca(2+)-regulatory proteins, i. e., troponin C, I and T, were prepared from puffer skeletal muscle. The SDS-gel electrophoretic study indicated that the molecular weights of troponin C, I and T were 18, 20 and 30k daltons, respectively. The Ca(2+)-sensitivity of the ATPase activity of the puffer myofibrils was abolished by the removal of troponin C by the CDTA-treatment and then restored by the reconstitution with puffer skeletal troponin C. The treatment with excess troponin T of either puffer or rabbit skeletal muscle at slightly acidic condition resulted in the removal of troponins C and I from the puffer myofibrils. The reconstituted puffer troponin C-I-T gave the Ca(2+)-sensitivity to the ATPase activity of puffer desensitized myofibrils in the presence tropomyosin.
钙调节蛋白,即肌钙蛋白C、I和T,是从河豚骨骼肌中制备的。SDS凝胶电泳研究表明,肌钙蛋白C、I和T的分子量分别为18、20和30千道尔顿。通过CDTA处理去除肌钙蛋白C可消除河豚肌原纤维ATP酶活性的钙敏感性,然后用河豚骨骼肌肌钙蛋白C重构可恢复其钙敏感性。在微酸性条件下,用过量的河豚或兔骨骼肌肌钙蛋白T处理会导致河豚肌原纤维中的肌钙蛋白C和I被去除。重构的河豚肌钙蛋白C-I-T在存在原肌球蛋白的情况下,赋予脱敏的河豚肌原纤维ATP酶活性钙敏感性。