原肌球蛋白
肌钙蛋白
肌钙蛋白C
化学
分馏
钙
肌钙蛋白I
生物化学
肌钙蛋白复合物
色谱法
肌动蛋白
有机化学
内科学
医学
心肌梗塞
作者
D.J. Hartshorne,Helmut Mueller
标识
DOI:10.1016/0006-291x(68)90610-4
摘要
The protein complex which governs the calcium sensitivity of natural actomyosin (Ebashi, 1963) has been shown to consist of two components, tropomyosin and troponin (Ebashi and Kodama, 1966; Hartshorne and Mueller, 1967). In the present study troponin has been separated into two distinct proteins, as judged by amino acid analyses. The fractionation was achieved at low pH and high ionic strength. One of the fractions, termed troponin B, effected a calcium insensitive inhibition of synthetic actomyosin ATPase activity, which was enhanced by the addition of tropomyosin. The other fraction, troponin A, conferred calcium sensitivity to the troponin B - tropomyosin system. The separation was reversible and all the properties of the source troponin were regained upon mixing troponin A and B in the correct proportions.
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