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Extra info for Biochemical Actions of Hormones. Volume 8
The inability to demonstrate the existence of soluble TN-C has made the observation of Dedman et al. (1977a) of questionable physiological significance. c. Calmodulin. Of all the Ca2+ receptors calmodulin has received the most intensive study (for a recent review, see Wang and Waisman, 1979). Calmodulin has been shown to exist in a variety of tissues within an organism (Smoake et ah, 1974) as well as in many different organisms including many plants and probably all animals (Waisman et ah, 1975; Charbonneau and Cormier, 1979; Waisman, 1979).
Recently Sherry et al. (1978) have demonstrated that once the RLC is phosphorylated, muscle contraction remains turned on in the absence of Ca2+, dephosphorylation of RLC by the myosin light chain phosphatase is required to turn muscle contractions off, a process (dephosphorylation) which is insensitive to Ca2+. Therefore, smooth muscle appears to be regulated by the cyclic phosphorylation and dephosphorylation of the RLC. , 1979). In skeletal and cardiac muscles the Ca2+-dependent phosphorylation of RLC is not believed to be directly involved in the regulation of muscle contraction.
1978) 1. 7 (J z < CÛ en O CO CÛ < 240 260 280 300 WAVELENGTH (nm) FIG. 5. Absorption spectra of earthworm modulator. 5 buffer containing 40 mM Tris/HCl, 1 mM MgAc2, and 50 μΜ CaCl2 was used. ) classes of binding sites appear to be present but there is no cooperativity in the binding of Ca2+ to these sites. y 1977). It appears that the structural and functional properties of calmodulin have been conserved phylogenetically. , 1978a) there is a remarkable 36 Howard Rasmussen and David Waisman similarity between this protein and the mammalian calmodulin (Table III).