1984/06/01 by DAVID A. HARRIS, David A. Harris, ARIEL A. SHERBANY +3
Medicine · Biochemistry, Genetics and Molecular Biology · #Cardiomyopathy and Myosin Studies #Muscle Physiology and Disorders #Cellular Mechanics and Interactions
paper · doi:10.2307/1541156
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.