The regulatory proteins of the myofibril. Separation and biological activity of the components of inhibitory-factor preparations.
1. Inhibitory-factor preparations isolated from myofibrils were shown to consist principally of proteins with molecular weights of 37000 and 23000. Under certain preparative procedures an additional component of molecular weight 14000 was present. 2. The 23000-dalton protein, the inhibitory factor, was the major active component. Its activity was enhanced by tropomyosin. 3. The 14000-dalton component also possessed inhibitory activity, although less than that of the 23000-dalton component when compared on a molar basis. Its activity was not always enhanced by tropomyosin. The 14000-dalton component could not be detected in whole fresh myofibrils and the limited evidence available is compatible with its formation during the preparation of the troponin complex. 4. The 37000-dalton component could not replace the inhibitory factor, calcium-sensitizing factor or tropomyosin as components of the relaxing-protein system. 5. All three components had distinctive amino acid compositions, particularly in their cysteine content.
D000205:Actomyosin; D000251:Adenosine Triphosphatases; D000595:Amino Acid Sequence; D000818:Animals; D002845:Chromatography; D002850:Chromatography, Gel; D003545:Cysteine; D004586:Electrophoresis; D008274:Magnesium; D008970:Molecular Weight; D009124:Muscle Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D009210:Myofibrils / Q000032:analysis*; D011817:Rabbits; D012967:Sodium Dodecyl Sulfate; D014335:Tropomyosin
D009124:Muscle Proteins; D014335:Tropomyosin; D012967:Sodium Dodecyl Sulfate; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D008274:Magnesium; D003545:Cysteine