Myosin from Molluscan Abalone, Haliotis discus

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Abstract
Actomyosin was extracted from smooth muscle of molluscan abalone with 0.1 M PP1 at pH 6.4. Myosin was separated from the actomyosin by centrifugation at 100,000×g in the presence of 5 mM ATP and 10 mM MgCl2 Myosin in the supernatant was further purified by gel filtration on a Sepharose 4B column. Paramyosin contamination of the actomyosin preparation interfered with the isolation of myosin and com plete removal of actin and paramyosin from the myosin has not been accomplished. The myosin appeared to consist of a single f-chain and a single g-chain, as examined by SDS-disc electrophoresis in 8 or 13.7% acrylamide gel. The ATPase [EC 3.6.1.3] activity of this myosin in 0.5 M KCl at neutral pH and at 0° was rather unstable and decreased by 10–20% per day. The effects of p-chloromercuri benzoate and EDTA on the ATPase activity were similar to those observed with other smooth muscle myosin but the dependence upon pH or KCl concentration was different.

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