An in vitro study of the interactions of skeletal muscle M-protein and creatine kinase with myosin and its subfragments.
Two proteins reported to be located in the M-band of skeletal muscle are M-protein (Mr 160,000) and creatine kinase (Mr 83,000). We have isolated and purified these proteins from adult chicken pectoralis muscle, and have studied their in vitro interactions with myosin, heavy meromyosin, light meromyosin and subfragment-2 in order to obtain a fuller understanding of the role these proteins play in the M-band of skeletal muscle. Experiments using the techniques of analytical ultracentrifugation, affinity chromatography and electron microscopy were carried out near physiological pH and ionic strength, under which conditions the M-band proteins are known to be firmly bound to the myofibril in situ. The results of our studies indicate that such interactions are either weak or absent in vitro. Discrepancies between our results and those from several other studies are discussed. We conclude that additional components may be required in order to observe interactions in vitro which are similar to those present in the intact myofibril.
D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D064211:Connectin; D003402:Creatine Kinase / Q000378:metabolism*; D066298:In Vitro Techniques; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism*; D015879:Myosin Subfragments / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D014461:Ultracentrifugation
D064211:Connectin; D009124:Muscle Proteins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D003402:Creatine Kinase; D009218:Myosins