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Extra info for Biochemical Actions of Hormones. Volume 8
The other, associated primarily with the duodenum has a molecular weight of 12,500 (Wasserman and Feher, 1977). Presumably, the later protein is similar to the 9700 dalton ICBP of bovine intestine sequenced by Hofman et al. (1977). This protein was also found to bind 2 mol C a 2 \ Ka 10"e-10-7. Besides the soluble ICBP of rat intestine Miller et al. (1979) have reported the existence of a particulate protein located in the brush borders of MW 18,500. They have suggested that this protein may be different than the soluble ICBP.
The trunk of the tree before this branching is thought to consist of the 4 EF containing ancestral protein. b. Troponin C. 1 μΜ in resting muscle to 10 μΜ in contracting muscle is the major event initiating muscle contraction. The molecular mechanisms by which Ca2+ regulates muscle contraction has been shown to involve two spatially distinct Ca2+ binding proteins; located on the thin filaments is troponin C (TN-C) and located on the thick filament is the myosin regulatory light chain (RLC). Muscle contraction is believed to be a consequence of the interaction of actln with the globular heads of myosin (for an excellent review, see Perry, 1979).
LeDonne and Coffee (1979) have demonstrated that pure parvalbumin does not activate PDE in a calcium-dependent fashion and that the results of Potter et ah (1977) were due to contamination of parvalbumin by calmodulin. Pechère et ah (1975) and Gillis and Gerday (1977) have suggested that parvalbumin may play a role in the relaxation cycle of white muscle. In particular, it has been suggested that parvalbumins may play the role of a shuttle mechanism for Ca2+ between myofibrils and the SR. In support of this suggestion is the observation that Ca2+ accumulation by SR is not fast enough to account for the rate of relaxation of a living muscle (Ebashi, 1976).