Actin-stimulated myosin Mg2+-ATPase inhibition by brain protein.
A low-molecular-weight protein, isolated from bovine brain, inhibits the actin-stimulated Mg-ATPase activity of myosin from striated muscle. This inhibition is probably related to its ability to cause actin to revert from its polymerized to its depolymerized state and to prevent the polymerization of actin. Its effect on the polymeric state of the actin has been demonstrated by viscosity studies. DNase inhibition assay, and electron microscopy. Heavy meromyosin can overcome the effect of the brain protein and stimulate the polymerization of actin. The inhibition of ATPase activity is in part dependent upon the relative amounts of brain protein, actin, and myosin. The apparent molecular weight of the brain protein is approximately 20,000 daltons. It appears to be a heat-labile glycoprotein containing 5-6% carbohydrate.
D000199:Actins / Q000502:physiology*; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000818:Animals; D001921:Brain / Q000502:physiology*; D017301:Ca(2+) Mg(2+)-ATPase; D002417:Cattle; D007700:Kinetics; D008854:Microscopy, Electron; D009218:Myosins / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D011485:Protein Binding; D011817:Rabbits
D000199:Actins; D009419:Nerve Tissue Proteins; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins