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Target molecular weight of the gastric (H+ + K+)-ATPase functional and structural molecular size. by G. Saccomani; G. Sachs; J. Cuppoletti; C.Y. Jung is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The state of assembly of the (H+ + K+)-ATPase in purified hog gastric mucosa membranes was studied by target size analysis applied to radiation-induced enzyme inactivation and polypeptide degradation data. Radiation inactivated the Mg2+-ATPase, K+-stimulated ATPase, and p-nitrophenyl phosphatase activities of the membrane preparation with a dose dependence characteristic of a target size of 270,000-daltons. Radiation also bleached the major 100,000-dalton sodium dodecyl sulfate-gel electrophoresis band of this preparation, indicating a radiation-induced degradation. This apparent polypeptide degradation exhibited a dose dependency corresponding to a target size of 250,000 daltons in situ. It is suggested that the gastric ATPase is a trimeric assembly of the 100,000-dalton polypeptides.

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Author

G. Saccomani; G. Sachs; J. Cuppoletti; C.Y. Jung

Publisher

Elsevier BV

Published

1981

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)