Dialdehyde ATP derivative as an affinity modifier of the Na+,K+-ATPase active site

L. R. Bernikov, K. N. Dzhandzhugazayan, Svetlana Lutsenko, N. N. Modyanov

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Abstract

Interaction of Na+,K+-ATPase from pig kidney in various conformational states with the dialdehyde analogue of ATP, α,α-(9-adenyl)-α'-D-(hydroxymethyl)diglycolaldehyde triphosphate ester (oATP), has been studied. This interaction leads to an enzyme modification which was shown to be of the affinity type according to the following criteria. 1. oATP can be hydrolyzed by Na+,K+-ATPase and prevent inhibition of ATPase activity by γ-[4-(N-2-chloroethyl-N-methylamino)]benzylamide ATP, indicating that it interacts with Na+,K+-ATPase in the enzyme active site. 2. oATP irreversibly inhibits ATP-hydrolyzing activity of Na+,K+-ATPase; the extent of inactivation is decreased in the presence of 20 mM ATP and depends on the ion composition of the modification medium. The inhibition and ATP protection are maximal in Na+,Mg2+-containing buffer. 3. The value of [14C]oATP incorporation into the α subunit is proportional to the degree of enzyme inactivation at low (

Original languageEnglish (US)
Pages (from-to)413-421
Number of pages9
JournalEuropean Journal of Biochemistry
Volume194
Issue number2
StatePublished - 1990
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Bernikov, L. R., Dzhandzhugazayan, K. N., Lutsenko, S., & Modyanov, N. N. (1990). Dialdehyde ATP derivative as an affinity modifier of the Na+,K+-ATPase active site. European Journal of Biochemistry, 194(2), 413-421.