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REGULATORY EFFECTS OF POTASSIUM ON (N a + + K + )‐ACTIVATED ADENOSINETRIPHOSPHATASE *
Author(s) -
Siegel G. J.,
Goodwin B. B.,
Hurley M. J.
Publication year - 1974
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1974.tb19092.x
Subject(s) - library science , annals , medicine , classics , history , computer science
The purpose of this paper is t o describe evidence that potassium ion can inhibit an early step in the reaction of nucleotide with (Na+ + K+)-activated ATPase; in addition it possesses the well known effect of activating enzyme dephosphorylation. There are two lines of evidence that bear on this issue. One comprises the observations of K+ inhibition of hydrolysis under certain conditions and the other derives from effects of K+ on ouabain binding to the enzyme. For the purposes of discussion, the magnesium-dependent, (Na' + K)stimulated ATP hydrolysis is written for each active enzyme subunit as follows. The support for this enzyme reaction model has been discussed previously.'