Castellani L, Vibert P
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.
J Muscle Res Cell Motil. 1992 Apr;13(2):174-82. doi: 10.1007/BF01874154.
Myosin co-assembles with paramyosin in the thick filaments of invertebrate muscles. The molar ratio of the two proteins varies greatly but where sufficient paramyosin is present it forms the filament core with myosin arranged on its surface. In the fastest acting striated muscles, paramyosin is present in small amounts, and neither its location nor the nature of its interactions with myosin has previously been established. Antibodies to paramyosin have now been used in an attempt to locate the protein in thick filaments that have been isolated from the striated adductor muscle of the scallop and then frayed apart into their constituent subfilaments. Using a gold-conjugated secondary antibody, the location of paramyosin in relation to the subfilaments has been determined by electron microscopy of negatively stained samples. The labelling indicates that paramyosin extends throughout the length of the scallop filaments and appears to be associated with each subfilament, raising the possibility that in these filaments paramyosin may not be confined to a central core domain.
肌球蛋白与副肌球蛋白在无脊椎动物肌肉的粗肌丝中共同组装。这两种蛋白质的摩尔比差异很大,但在有足够副肌球蛋白存在的情况下,它形成丝芯,肌球蛋白排列在其表面。在收缩速度最快的横纹肌中,副肌球蛋白含量很少,其位置以及与肌球蛋白相互作用的性质此前均未确定。现在,针对副肌球蛋白的抗体已被用于尝试在从扇贝横纹内收肌分离出来、然后拆分成其组成亚丝的粗肌丝中定位该蛋白质。使用金标记的二抗,通过对负染样品进行电子显微镜观察,确定了副肌球蛋白相对于亚丝的位置。标记表明副肌球蛋白贯穿扇贝肌丝的全长,并且似乎与每条亚丝相关联,这增加了在这些肌丝中副肌球蛋白可能不限于中央核心区域的可能性。