肌原纤维的调节蛋白。钙敏化因子（肌钙蛋白A）的特性与生物活性
The regulatory proteins of the myofibril. Characterization and biological activity of the calcium-sensitizing factor (troponin A).
作者信息
Schaub M C, Perry S V, Häcker W
出版信息
Biochem J. 1972 Jan;126(1):237-49. doi: 10.1042/bj1260237.
Abstract
- Electrophoretically homogeneous calcium-sensitizing factor was prepared from the troponin complex by chromatography successively on sulphoethyl-Sephadex and on diethyl-(2-hydroxypropyl)aminoethyl-Sephadex in 6m-urea. It is a protein containing 53% of polar amino acids, of which a net excess consists of acidic residues. 2. On gel filtration the calcium-sensitizing factor was shown to be the only myofibrillar protein that bound (45)Ca(2+) tightly in the presence of 2-6m-urea. 3. Calcium-sensitizing factor effectively neutralized the effect of the inhibitory factor on the ATPase activities of actomyosin systems. Tropomyosin was essential for the regulation, by changes in the Ca(2+) concentration, of the neutralizing effect of calcium-sensitizing factor on the inhibitory factor. 4. Prolonged exposure to chelators of Ca(2+) produced an irreversibly modified form of calcium-sensitizing factor of higher electrophoretic mobility at pH8.6. The modified form neutralized the inhibitory factor action but this property could no longer be controlled by the Ca(2+) concentration in the presence of tropomysin. 5. The calcium-sensitizing factor and tropomyosin could be replaced by their carboxymethylated derivatives in the relaxing-protein system.
摘要
- 通过在6m尿素中先后在磺乙基葡聚糖凝胶和二乙基-(2-羟丙基)氨乙基葡聚糖凝胶上进行层析，从肌钙蛋白复合物中制备出电泳均一的钙敏化因子。它是一种含有53%极性氨基酸的蛋白质，其中净过量部分由酸性残基组成。2. 在凝胶过滤中，钙敏化因子被证明是唯一一种在2 - 6m尿素存在下能紧密结合(45)Ca(2+)的肌原纤维蛋白。3. 钙敏化因子有效地中和了抑制因子对肌动球蛋白系统ATP酶活性的影响。原肌球蛋白对于通过改变Ca(2+)浓度来调节钙敏化因子对抑制因子的中和作用至关重要。4. 长时间暴露于Ca(2+)螯合剂会产生一种在pH8.6时电泳迁移率更高的不可逆修饰形式的钙敏化因子。这种修饰形式中和了抑制因子的作用，但在原肌球蛋白存在的情况下，这种特性不再受Ca(2+)浓度控制。5. 在松弛蛋白系统中，钙敏化因子和原肌球蛋白可以被它们的羧甲基化衍生物所替代。
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