Purification of a troponin I-like factor from pig platelet.
A troponin I-like factor has been purified from pig platelet by G150 Sephadex filtration of a low ionic strength extract, acidification at pH 4.2, ion exchange on DE-52 cellulose, and affinity chromatography on calmodulin-Sepharose. This protein (Mr 17000), together with pig brain calmodulin and platelet tropomyosin, is able to participate to the reconstitution in vitro of a thin filament-like complex which modulates with 55% calcium sensitivity the platelet actin-activated Mg2+-dependent ATPase activity of rabbit skeletal muscle myosin.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors; D000818:Animals; D001792:Blood Platelets / Q000032:analysis*; D017301:Ca(2+) Mg(2+)-ATPase; D002118:Calcium / Q000502:physiology; D002147:Calmodulin / Q000378:metabolism; D066298:In Vitro Techniques; D009124:Muscle Proteins / Q000097:blood*; D009132:Muscles / Q000201:enzymology; D011485:Protein Binding; D013552:Swine; D014335:Tropomyosin / Q000494:pharmacology; D014336:Troponin / Q000097:blood* / Q000494:pharmacology; D019210:Troponin I
D002147:Calmodulin; D009124:Muscle Proteins; D014335:Tropomyosin; D014336:Troponin; D019210:Troponin I; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D002118:Calcium