Key result
Myosin isoenzymes enriched in either alkali 1 or alkali 2 light chains exhibited nearly identical maximum rates of ATP hydrolysis and similar apparent affinities for actin.
Population
Myosin isoenzymes enriched in either alkali 1 or alkali 2 light chains
Comparison
Light chain exchange in 4.7 M ammonium chloride vs Comparison between alkali 1 and alkali 2…
Design
Preclinical
Authors
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Similar ATPase kinetics between light-chain variants leaves open distinct regulatory roles in cardiac myosin function.
The presence of a specific alkali light chain does not significantly influence the maximum rate of ATP turnover by actomyosin under near-physiological ionic strength conditions.
Pope et al. (1981) studied this question. Myosin isoenzymes enriched in alkali 1 or alkali 2 light chains was evaluated on Maximum rates of ATP hydrolysis and apparent affinities for actin. Myosin isoenzymes enriched in either alkali 1 or alkali 2 light chains exhibited nearly identical maximum rates of ATP hydrolysis and similar apparent affinities for actin.
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