Key result
Smooth muscle actin preparations showed a 2.5-fold higher Kapp for myosin ATPase activation compared to sarcomeric actins, correlating with amino acid substitutions at positions 17 and 89.
Authors
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May influence isoform-specific contractile properties; leaves open in vivo relevance of positions 17 and 89.
Mossakowska et al. (1985) studied Actin-myosin interaction. Smooth muscle actin (bovine aorta, chicken gizzard) vs. Sarcomeric muscle actin (bovine cardiac, rabbit skeletal) was evaluated on Mg2+-ATPase activity (Vmax and Kapp). Smooth muscle actin preparations showed a 2.5-fold higher Kapp for myosin ATPase activation compared to sarcomeric actins, correlating with amino acid substitutions at positions 17 and 89.