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从丝瓜 (Luffacylindrica (L .)Roem .)卷须中纯化得到分子量为 174kD的肌球蛋白 ,并对其进行了酶学与电子显微学的研究。这种肌球蛋白具有肌动蛋白激活的MgATPase活性 ,能够被抗动物肌肉的肌球蛋白的单克隆抗体识别。电子显微学研究表明 :它有两个头部 (大小和形状与动物肌肉的肌球蛋白相似 )和一条相对较短的尾部。还对丝瓜卷须的肌动蛋白进行了观测 ,偶尔发现一些尾部有球状结构的肌球蛋白。该肌球蛋白的免疫特性和超微结构证明了它由 2条重链组成 ,并与传统的肌球蛋白相似。然而 ,这种 174kD的肌球蛋白是否参与了丝瓜的接触卷曲有待于进一步研究。
Myosin with a molecular weight of 174 kD was purified from tendril of Luffacylindrica (L.) Roem., And its enzymatic and electron microscopic studies were performed. This myosin has actin-activated MgATPase activity and is recognized by monoclonal antibodies to myosin in animal muscles. Electron microscopy studies have shown that it has two heads (similar in size and shape to myosin in animal muscles) and a relatively short tail. The actin of loofah tendril was also observed, and occasionally some myosin with a globular structure was found. The myosin’s immunogenicity and ultrastructure demonstrate that it consists of two heavy chains and is similar to the traditional myosin. However, whether this 174 kD myosin is involved in the contact curl of loofah remains to be further studied.