intTypePromotion=1
zunia.vn Tuyển sinh 2024 dành cho Gen-Z zunia.vn zunia.vn
ADSENSE

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

45
lượt xem
5
download
 
  Download Vui lòng tải xuống để xem tài liệu đầy đủ

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. ...

Chủ đề:
Lưu

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

ADSENSE

CÓ THỂ BẠN MUỐN DOWNLOAD

 

Đồng bộ tài khoản
9=>0