The structural differences in the N-terminal regions of regulatory light chains a and b may explain their functional differences in inducing catch contraction in scallop smooth muscle.
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May explain functional divergence in scallop catch contraction; hypothesis-generating for light-chain isoforms in mammalian cardiovascular research.
Smooth muscle myosin from scallop (Patinopecten yessoensis) adductor muscle contains two kinds of regulatory light chains (regulatory light chains a and b), and myosin having regulatory light chain a is suggested to be suitable for inducing "catch contraction" rather than myosin having regulatory light chain b (Kondo, S. & Morita, F. (1981) J. Biochem. 90, 673-681). The amino acid sequences of these two light chains were determined and compared. Regulatory light chain a consists of 161 amino acid residues, while regulatory light chain b consist of 156 amino acid residues. Amino acid substitutions and insertions were found only in the N-terminal regions of the sequences. The structural difference between the two light chains may contribute to the functional difference between myosins having regulatory light chains a and b.
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Miyanishi et al. (1985) studied this question.
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