Key result
Affinity chromatography of bovine brain cortex yielded three troponin components (I, C, and T) with apparent molecular weights of 18,700, 14,000, and 36,400, respectively.
The brain actomyosin complex may be regulated in a manner similar to striated muscle actomyosin via analogous troponin subunits.
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Troponin-like proteins in brain may regulate actin-myosin; leaves open functional roles in neurons.
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.
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Mahendran et al. (1979) studied this question. Affinity chromatography was evaluated on Isolation and characterization of brain troponin complex components. Affinity chromatography of bovine brain cortex yielded three troponin components (I, C, and T) with apparent molecular weights of 18,700, 14,000, and 36,400, respectively.
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