Comparative studies on myosin ATPase of a flying and nonflying bird.
Myosin was purified from the flight muscles of a flying (pigeon) and a nonflying (fowl) bird. Ki (ADP) of myosin ATPase of pigeon is higher, but the Km (ATP) is lower than that of fowl. The specific activity (mumole of Pi liberated/min/mg protein) is higher for the fowl. A0.5 (CaCl2) of myosin of both pigeon and fowl is similar. However, the two proteins differ in their interactions with ADP, ATP and p-chloromercuribenzoate. The two proteins have the same tyrosine, tryptophan and sulfhydryl contents. The electrophoretic patterns of the two myosins on SDS-polyacrylamide gels are different. These studies show significant molecular differences in the myosin derived from the flight muscles of a flying (pigeon) and a nonflying (fowl) bird.
D000222:Adaptation, Physiological; D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate; D000818:Animals; D001717:Birds / Q000502:physiology*; D002122:Calcium Chloride / Q000494:pharmacology; D002645:Chickens; D002729:Chloromercuribenzoates / Q000494:pharmacology; D010856:Columbidae; D004789:Enzyme Activation / Q000187:drug effects; D005426:Flight, Animal; D009132:Muscles / Q000201:enzymology* / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*
D002729:Chloromercuribenzoates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins; D002122:Calcium Chloride