Nature of adenosine triphosphatase accelerating peptide from hydrolysate of fur seal muscle.
Ultrafiltered fur seal muscle hydrolysate was divided into eleven fractions by gel filtration on Sephadex G-15. One of the fractions (Fraction G9) accelerated the ATPase activity of carp myosin B to a rate about two-fold faster than that of the control. Fraction G9 showed a single ninhydrin spot in its silica gel thin layer chromatograph, and gave a positive test for tryptophan by the p-dimethylaminobenzaldehyde method, while tests for tyrosine, and for arginine were negative. The ion exchange amino acid analysis of its acid hydrolysate showed a predominant content of lysine, nearly equivalent to the amount of tryptophan determined from its UV absorbancy and the p-dimethylaminobenzaldehyde method. The N-terminal amino acid analysis gave di-DNP-Lys as the sole DNP-amino acid. The structure of the ATPase accelerating peptide fraction, Fraction G9, was deduced to be Lys-Trp.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D010872:Caniformia / Q000378:metabolism*; D002347:Carps; D004151:Dipeptides / Q000302:isolation & purification / Q000502:physiology*; D004789:Enzyme Activation; D046069:Fur Seals / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D009218:Myosins / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet
D004151:Dipeptides; D000251:Adenosine Triphosphatases; D009218:Myosins