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RESOLUTION OF BRAIN TROPONIN COMPLEX
Author(s) -
Mahendran C.,
Berl S.
Publication year - 1979
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.1471-4159.1979.tb11717.x
Subject(s) - troponin c , troponin , myosin , skeletal muscle , egta , actin , sephadex , troponin t , biochemistry , chemistry , cardiac muscle , affinity chromatography , biology , calcium , anatomy , medicine , enzyme , organic chemistry , myocardial infarction
Affinity chromatography was used to partially purify the troponin complex from crude regulatory proteins obtained from bovine brain cortex. Three components were obtained from this partially purified troponin complex by treatment with 6 M‐urea and 1 mM‐EGTA followed by chromatography on DEAE‐Sephadex‐A50. The effects of the three components on skeletal muscle actin activated MgATPase activity of muscle myosin (ATP phosphohydrolase, EC 3.6.1.3.) suggested that they were analogous to that of the skeletal muscle troponins I, C, and T. The apparent molecular weights of the brain troponin subunits (I, C, and T) were 18, 700, 14, 000 and 36, 400, respectively. The molecular weights of the former two proteins were less than those reported for the analogous skeletal muscle troponins. Thus, brain actomyosin complex may be regulated in a manner similar to that of striated muscle actomyosin.