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- W168078723 abstract "This chapter discusses the effects of Ca-binding proteins and biogenic amines. Cyclic AMP-dependent protein kinase phosphorylates both synaptic and microsomal membrane proteins. In the presence of Ca, the phosphorylation of these membranes is increased. An increased level of phosphorylation is coupled with the activation of Mg, Ca-ATPase, and uptake of 45Ca by microsomes. At the low concentration of Ca2+, an acidic protein, with a molecular weight of 9000, is released from the membranes. This protein binds Ca ions and is heat stable. It inhibits both membrane bound and cytosolic cyclic AMP-dependent protein kinases. When the concentration of Ca is decreased, this modulator protein released from the membranes leads to the inhibition of soluble protein kinase, phosphorylation of membrane, and activity of Mg,Ca-ATPase. Increasing of the concentration of Ca caused linkage of this protein with membrane and activation of Mg,Ca-ATPase. It is revealed that interaction between biogenic amines and Mg,Ca-ATPase is realized not only by cyclic nucleotides. The results demonstrate that biogenic amines act directly on ATPase." @default.
- W168078723 created "2016-06-24" @default.
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- W168078723 date "1980-01-01" @default.
- W168078723 modified "2023-09-25" @default.
- W168078723 title "ON EFFECTS OF Ca-BINDING PROTEINS AND BIOGENIC AMINES" @default.
- W168078723 doi "https://doi.org/10.1016/b978-0-08-025921-5.50063-1" @default.
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