[Affinity modification of heavy meromyosin and subfragment 1 by mixed anhydrides of [14C] AMP, epsilon AMP and mesitylene carboxylic acid].
Using mixed anhydride of AMP and mesitylene carboxylic acid carrying a fluorescent or radioactive label, it was found that the previously established irreversible inhibition of myosin ATPase is a result of protein covalent binding to the nucleotide residue of the inhibitor. The stoichiometry of the affinity labelling of heavy meromyosin is 1 mole of nucleotide residue of mixed anhydride per 1 mole of protein, that of subfragment 1-0.5 mole per 1 mole of protein. The lack of irreversible inhibition of the ATPase activity of subfragment 1 is suggestive of an existence of a regulatory substrate-binding site in the myosin molecule.
D000249:Adenosine Monophosphate / Q000031:analogs & derivatives; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000345:Affinity Labels / Q000494:pharmacology*; D000812:Anhydrides; D000818:Animals; D001555:Benzene Derivatives; D015879:Myosin Subfragments / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D051381:Rats; D013050:Spectrometry, Fluorescence; D014992:Xylenes / Q000494:pharmacology
D000345:Affinity Labels; D000812:Anhydrides; D001555:Benzene Derivatives; D015879:Myosin Subfragments; D010446:Peptide Fragments; D014992:Xylenes; C030368:etheno-AMP; D000249:Adenosine Monophosphate; C010219:mesitylene; D000251:Adenosine Triphosphatases; D009218:Myosins
Affinnaia modifikatsiia tiazhelogo meromiozina i subfragmenta-1 smeshannymi angidridami [14C] AMP, epsilonAMP i mexitilenkarbonovoĭ kisloty.