Kuroda M, Maruyama K
J Biochem. 1976 Aug;80(2):315-22. doi: 10.1093/oxfordjournals.jbchem.a131279.
A new regulatory protein which we have designated as gamma-actinin has been isolated from native thin filaments of rabbit skeletal muscle. Depolymerized native thin filaments were fractionated by salting out with ammonium sulfate, and the precipitates obtained at 40--60% ammonium sulfate saturation were further subjected to DEAE-Sephadex and Sephadex G-200 column chromatography. The purified gamma-actinin was shown to have a chain weight of 35,000 daltons and had a strong inhibitory action on the polymerization of G-actin. The results of amino acid analysis indicated a unique amino acid composition of gamma-actinin as compared with other structural proteins of muscle. Non-polar and neutral amino acid residues were abundant. One cysteine residue was contained per one molecule of gamma-actinin and played a critical role in the maintenance of the inhibitory activity. Pelleting of gamma-actinin with F-actin showed that gamma-actinin binds to F-action.
我们已从兔骨骼肌的天然细肌丝中分离出一种新的调节蛋白，我们将其命名为γ - 辅肌动蛋白。通过用硫酸铵盐析对解聚的天然细肌丝进行分级分离，在硫酸铵饱和度为40 - 60%时获得的沉淀物进一步进行DEAE - 葡聚糖凝胶和葡聚糖凝胶G - 200柱色谱分析。纯化后的γ - 辅肌动蛋白显示其链重为35,000道尔顿，对G - 肌动蛋白的聚合具有强烈的抑制作用。氨基酸分析结果表明，与肌肉的其他结构蛋白相比，γ - 辅肌动蛋白具有独特的氨基酸组成。非极性和中性氨基酸残基丰富。每分子γ - 辅肌动蛋白含有一个半胱氨酸残基，该残基在维持抑制活性中起关键作用。γ - 辅肌动蛋白与F - 肌动蛋白的沉淀表明γ - 辅肌动蛋白与F - 肌动蛋白结合。
