Temperature-dependent transitions of the myosin-product intermediate at 10.DEG. during Mn(II)-ATP hydrolysis by myosin from rabbit psoas muscle.

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説明

The initial burst of Pi liberation during the hydrolysis of Mn(II)-ATP by heavy meromyosin from rabbit psoas muscle was investigated. Below 10°, the initial burst of Pi liberation was inhibited by the pre-addition of ADP without any change in the steady-state activity, but it was not inhibited above 10°. The burst size was about one mole per mole of heavy meromyosin. The initial burst of Pi liberation in Mg-ATP hydrolysis at 8°, however, was not inhibited by the pre-addition of ADP.These results, obtained with psoas muscle heavy meromyosin, were almost the same as those obtained with heavy meromyosin from rabbit leg and back muscles (Hozumi & Tawada (1975) Biochim. Biophys. Acta 376, 1-12) and, therefore, indicate that in Mn-ATP above 10& there is at the burst site a predominant myosin*-product complex generated by ATP hydrolysis. Similarly, below 10& there is a myosin-product complex identical with the one generated by adding ADP (and Pi) to myosin.

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