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- W153919708 abstract "This chapter elaborates a comparison made of the characteristics of the activations by acidic phospholipids and controlled trypsinolysis. The pattern of trypsin proteolysis is described in some detail, with particular attention to the reconstitution of fragments in liposomes and to the effects of trypsin on the calmodulin binding domain of the molecule. The effects of chymotrypsin and calpain on the binding of calmodulin to the ATPase and on the organization of the domain that interacts with the activator are also discussed in the chapter. Chymotrypsin activates the purified ATPase much more rapidly than trypsin. Calpain is a relatively novel protease, which has been shown to attack several membrane proteins. Recent carboxypeptidase digestion experiments on the ATPase in situ support the suggestion, and the demonstration that the calmodulin binding domain of myosin light chain kinase is located in the C-terminus region suggest a tempting analogy. It is hoped that work on the primary structure of the ATPase, under way in several laboratories, will support these predictions with conclusive experimental data." @default.
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- W153919708 date "1987-01-01" @default.
- W153919708 modified "2023-10-02" @default.
- W153919708 title "THE CALCIUM PUMP OF THE PLASMA MEMBRANE: RECENT STUDIES ON THE PURIFIED ENZYME AND ON ITS PROTEOLYTIC FRAGMENTS, WITH PARTICULAR ATTENTION TO THE CALMODULIN BINDING DOMAIN" @default.
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- W153919708 doi "https://doi.org/10.1016/b978-0-12-521040-9.50015-2" @default.
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