Maruyama K, Kamiya R, Kimura S, Hatano S
J Biochem. 1976 Apr;79(4):709-15. doi: 10.1093/oxfordjournals.jbchem.a131122.
A beta-actinin-like protein was isolated from plasmodia of the slime mold. The chain weight was the same as that of actin (43,000), but the amino acid composition was significantly different. The action of plasmodium beta-actinin on actin was the same as that of beta-actinin from rabbit skeletal muscle: inhibition of the recombination of F-actin fragments; formation of Mg polymer; inhibition of interfilamental interaction of F-actin and retardation of depolymerization of F-actin. The only difference observed was its sensitivity to trypsin: plasmodium actinin was less quickly digested by trypsin than rabbit beta-actinin.
从黏菌的原质团中分离出一种类β-辅肌动蛋白。其链重与肌动蛋白相同(43,000),但氨基酸组成明显不同。疟原虫β-辅肌动蛋白对肌动蛋白的作用与兔骨骼肌β-辅肌动蛋白相同:抑制F-肌动蛋白片段的重组;形成镁聚合物;抑制F-肌动蛋白的丝间相互作用并延缓F-肌动蛋白的解聚。观察到的唯一差异是其对胰蛋白酶的敏感性:疟原虫辅肌动蛋白被胰蛋白酶消化的速度比兔β-辅肌动蛋白慢。