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Japanese journal of pharmacology

Effect of peptide bond splitting on ouabain sensitive conformational changes in Na+,K+-ATPase treated with N-[p-(2-benzimidazolyl)phenyl]maleimide.


PMID 3033363

Abstract

Trypsin treatment of N-[p-(2-benzimidazolyl)phenyl]maleimide modified enzyme caused a marked reduction in Na+,K+-ATPase activity and in the amount of the alpha-chain, which contains the phosphorylation and ouabain binding sites. However, these preparations retained nearly 90% of the ouabain binding capacity and showed ouabain sensitive dynamic fluorescence changes accompanying the hydrolysis of ATP. The data showed that the three dimensional structure of Na+,K+-ATPase, which is important in the dynamic fluorescence change, is little affected in spite of extensive covalent bond splitting in the alpha-chain of Na+,K+-ATPase.