Effect of Peptide Bond Splitting on Ouabain Sensitive Conformational Changes in Na+, K+-ATPase Treated with N-[p-(2-Benzimidazolyl)phenyl]maleimide

[摘要] References(19)Cited-By(2)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 α-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 a-chain of Na+, K+ATPase.

[学科分类] 药理学