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TitleOccurrence and Characteristics of {sup 18}O-exchange Reactions Catalyzed By Sodium- and Potassium-dependent Adenosine Triphosphatases
Author(s)Dahms, A. S.; Boyer, P. D.
Publication Date1972
Report NumberUCLA--34-P-102-36
Unique IdentifierACC0191
Other NumbersOSTI ID: 4485348
Research OrgUniversity of California, Los Angeles (USA)
Contract NoAT(04-3)-34
Sponsoring OrgU.S. Atomic Energy Commission (AEC)
SubjectN40230 -- Chemistry -- Inorganic, Organic, & Physical Chemistry -- Isotope Exchange & Isotope Separation; Oxygen 18 -- Isotopic Exchange; ATP-ASE; Catalysis; Chemical Reaction Kinetics; Potassium Compounds; Sodium Compounds; Water
Related Web PagesPaul D. Boyer, Adenosine Triphosphate [ATP], and the Binding Change Mechanism
AbstractMicrosomal preparations of the (Na{sup +},K{sup +}-ATPase from porcine outer medulla and electroplax catalyzed a rapid Mg{sup 2+}- and K{sup +}-dependent exchange of water oxygens with inorganic phosphate in the absence of ATP or ADP. Exchange activity was unaffected by uncouplers and inhibitors of oxidative phosphorylation but was inhibited by Na{sup +}, ouabain, N,N'-dicyclohexylcarbodiimide, or p-mercuribenzoate. No nucleotide requirement for the exchange could be demonstrated. Addition of ATP to Na{sup +}-inhibited system resulted in an exchange of oxygens of medium P{sub i} concomitant with ATP hydrolysis. This ATP-induced exchange amounted to 1.5 oxygen atoms per P{sub i} released. Neither ADP nor adenylyl methylene diphosphonate would serve to activate the exchange.
1475 K
45 pp.
 
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