Effects of tryptic digestion on the enzymatic activites of chicken gizzard myosin.
Tryptic digestion of gizzard myosin resulted in the degradation of the 20K light chain (G1) to its 17K fragment, which could not be phosphorylated. The rapid loss of Ca2+-dependent activation of actomyosin ATPase activity accompanied the degradation of G1. Increase in the Ca2+-ATPase activity and decrease in the EDTA-ATPase activity of myosin accompanied the degradation of myosin heavy chain, but not the cleavage of G1.
D000199:Actins / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002645:Chickens; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D005895:Gizzard, Avian / Q000201:enzymology*; D009218:Myosins / Q000378:metabolism* / Q000494:pharmacology; D010446:Peptide Fragments / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism*
D000199:Actins; D010446:Peptide Fragments; D010710:Phosphates; D004492:Edetic Acid; D014357:Trypsin; D000251:Adenosine Triphosphatases; D009218:Myosins; D002118:Calcium