Abstract
The extraction of protein from the striated muscle (prerigor and postrigor) of scallop (Placopecten magellanicus) by salt solutions of various strengths and at pH 7 was investigated. With postrigor muscle the structural proteins appeared in the extract only at ionic concentrations (Γ/2) greater than 0.3.With prerigor muscle, most of the protein was extracted at Γ/2 = 0.15. A large part of this protein precipitated from the extract upon standing, and when redissolved in stronger salt solutions resembled myosin B in sedimentation behavior and ultraviolet absorption.
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