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Biol Bull 166: 482-493. (June 1984)
© 1984 Marine Biological Laboratory
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PURIFICATION AND CHARACTERIZATION OF MUSCLE PROTEINS FROM APLYSIA CALIFORNICA

DAVID A. HARRIS 1, ARIEL A. SHERBANY 1, and JAMES H. SCHWARTZ 1

1 Center for Neurobiology and Behavior and Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, New York, New York 10032

We report the purification and characterization of the major contractile proteins from body wall muscle of the marine mollusc Aplysia californica, and have found that they are quite similar to those of other molluscs. Myosin from this animal consists of heavy chains and at least two different classes of light chains; like the enzymatic activity of other molluscan myosins, its ATPase activity is regulated by Ca++. Actin can be prepared from thin filaments by procedures that minimize denaturation of the protein. Aplysia tropomyosin consists of two subunits with apparent molecular weights of 33,000 and 37,000. Paramyosin migrates as a polypeptide of molecular weight 100,000. A description of the procedures for purifying these proteins from Aplysia may be useful to neurobiologists who are now using this animal extensively.

Submitted on March 6, 1984
Accepted on March 23, 1984




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[Abstract] [Full Text] [PDF]


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