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Gerald Litwack's Biochemical Actions of Hormones. Volume 8 PDF

By Gerald Litwack

ISBN-10: 0124528082

ISBN-13: 9780124528086

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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. Ueng and Bronner (1979) have used the counter ion electrophoresis to identify the ICBP of rat intestine and have concluded that under conditions in which proteolysis is controlled only one soluble ICBP may exist.

1978). They are present in especially large amounts in the skeletal muscles of vertebrates (Table I). Results of tissue distribution studies (Baron et ah, 1975) have suggested that the majority of parvalbumin molecules within an organism are located in the white muscle, but are not restricted to this tissue. a. sequence of a variety of parvalbumins has revealed that they are isostructural (Kretsinger, 1980). The physiological function of parvalbumin is at present unknown. Potter et ah (1977) have suggested that parvalbumin may play a role in the activation of PDE.

Myosin Essential Light Chain. The essential light chains (ELC) of myosins cannot be phosphorylated nor do they bind Ca 2+ . Their function remains largely unknown. Wagner and Yount (1976) have reported that chemical modification of the single serine residue in the ELC of skeletal and cardiac muscle inhibits both ATP hydrolysis and actin binding. Wagner et al. (1979) have analyzed the possible role of the alkali light chains in the actin-activated ATPase of myosin subfragment. They have cautiously suggested that the ELC may play a role in influencing the kinetic properties of the actin-activated ATPase.

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Biochemical Actions of Hormones. Volume 8 by Gerald Litwack

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