Calcium-sensitive modulation of the actomyosin ATPase by fodrin.

作者: P D Wagner

DOI: 10.1016/S0021-9258(20)82141-3

关键词:

摘要: Fodrin, a spectrin-like protein isolated from brain, is long flexible molecule which binds calmodulin and cross-links F-actin. The effects of fodrin on the actin-activated ATPase myosin have been examined. When added after ATP, inhibited actomyosin ATPase. Two to three times as much was required for inhibition in presence Ca2+ its absence. Complete absence occurred at about one 200 actins. Inhibition does not appear result cross-linking F-actin, and, thereby, preventing filaments reaching actin filaments; but may promote by trapping within cross-linked before stimulated almost 3-fold less than 50% Ca2+. Stimulation thought After several minutes stimulations were greatly reduced, ATPases substantially inhibited. Whether or subfragment 1. This also slightly sensitive.

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