Separation of two different heavy meromyosins. Evidence for the presence of myosin isozymes in rabbit skeletal muscle.
Heavy meromyosin prepared from rabbit skeletal myosin by chymotryptic digestion was separated into two different heavy meromyosins by Sepharose 4B-6 aminohexyl PPi column chromatography. SDS-gel electrophoresis of one fraction of heavy meromyosin, which was eluted with 75 mM ammonium acetate, showed that it contained the small polypeptide chains, g3 and g2, as well as the large chains. The other fraction of heavy meromyosin, which was eluted with 85 mM ammonium acetate, contained g1 and g2. We concluded that the two heavy meromyosins arose from two different populations (isozymes) of myosin. No significant difference in Ca2+-ATPase activity was detected between the two heavy meromyosins.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification; D000818:Animals; D007527:Isoenzymes / Q000302:isolation & purification*; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D015879:Myosin Subfragments / Q000302:isolation & purification*; D009218:Myosins / Q000302:isolation & purification*; D011817:Rabbits
D007527:Isoenzymes; D015879:Myosin Subfragments; D000251:Adenosine Triphosphatases; D009218:Myosins