Natural dipeptides of skeletal muscles, carnosine (β-alanylhistidine) and anserine (β-alanyl-1-methylhistidine), have been demonstrated to be myosin ATPase activators, the latter being much more effective than the former under identical experimental conditions. At low ionic strengths of K+, Mg++, and Ca++ the activating effect of carnosine was marked at optimal concentration of ATP, and at levels of ATP in which there was apparent substrate inhibition the effect was very pronounced. The effect of carnosine appears to be specific rather than an ionic strength effect. The lowest concentrations of carnosine and anserine found to be activating were comparable to concentrations found in tissue.
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Avena et al. (1969) studied this question.
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