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Actin‐Stimulated Myosin Mg 2+ ‐ATPase Inhibition by Brain Protein
Author(s) -
Berl S.,
Chou M.,
Mytilineou C.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb13582.x
Subject(s) - heavy meromyosin , myosin , actin , atpase , chemistry , biochemistry , polymerization , biophysics , myosin atpase , glycoprotein , electron microscope , microbiology and biotechnology , biology , enzyme , polymer , organic chemistry , physics , optics
A low‐molecular‐weight protein, isolated from bovine brain, inhibits the actin‐stimulated Mg‐ATPase activity of myosin from striated muscle. This inhibition is probably related to its ability to cause actin to revert from its polymerized to its depolymerized state and to prevent the polymerization of actin. Its effect on the polymeric state of the actin has been demonstrated by viscosity studies, DNase inhibition assay, and electron microscopy. Heavy meromyosin can overcome the effect of the brain protein and stimulate the polymerization of actin. The inhibition of ATPase activity is in part dependent upon the relative amounts of brain protein, actin, and myosin. The apparent molecular weight of the brain protein is approximately 20,000 daltons. It appears to be a heat‐labile glycoprotein containing 5–6% carbohydrate.