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Báo cáo khoa học: The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:14

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The structural stability of the large cytoplasmic domain (H4 -H5loop) of mouse a1subunit of Na + /K + ATPase (L354– I777), the number and the location of its binding sites for 2¢-3¢-O-(trinitrophenyl) adenosine 5¢-triphosphate (TNP-ATP) andp-nitrophenylphosphate (pNPP) were investi-gated. C- and N-terminal shortening revealed that neither part of the phosphorylation (P)-domain are necessary for TNP-ATP binding. There is no indication of a second ATP site on the P-domain of the isolated loop, even though others reported previously of its existence by TNP-N3ADP affinity labeling of the full enzyme. ...

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Nội dung Text: Báo cáo khoa học: The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site

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