Wallimann T, Pelloni G, Turner D C, Eppenberger H M
Proc Natl Acad Sci U S A. 1978 Sep;75(9):4296-300. doi: 10.1073/pnas.75.9.4296.
Column-purified antibodies against creatine kinase (EC 2.7.3.2) from chicken skeletal muscle (the homodimeric isoenzyme designated MM-CK) bind specifically to the M lines of chicken pectoral muscle myofibrils. Incubation of myofibrils with monovalent Fab' fragments of these antibodies solubilizes most of the myofibril-bound creatine kinase, concomitantly removing most of the electron-dense material from the M lines. This strongly indicates that MM-CK is an integral part of the M-line structure and is consistent with the suggestion that MM-CK molecules form the M bridges that are responsible for the principle M-line substriations.
从鸡骨骼肌中通过柱层析纯化得到的抗肌酸激酶(EC 2.7.3.2)抗体(针对同二聚体同工酶MM-CK)能特异性结合鸡胸肌肌原纤维的M线。用这些抗体的单价Fab’片段孵育肌原纤维,可使大部分与肌原纤维结合的肌酸激酶溶解,同时从M线去除大部分电子致密物质。这有力地表明MM-CK是M线结构的一个组成部分,并且与MM-CK分子形成负责M线主要亚条纹的M桥这一观点相一致。