Contribution to Tl+, K+, and Na+ Binding of Asn776, Ser775, Thr774, Thr772, and Tyr771 in Cytoplasmic Part of Fifth Transmembrane Segment in α-Subunit of Renal Na,K-ATPase-Reference-Cited by-同舟云学术

Contribution to Tl+, K+, and Na+ Binding of Asn776, Ser775, Thr774, Thr772, and Tyr771 in Cytoplasmic Part of Fifth Transmembrane Segment in α-Subunit of Renal Na,K-ATPase

Published:1998-12-01 Issue:51 Volume:37 Page:17818-17827
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Pedersen Per Amstrup¹,Nielsen Jesper M.¹,Rasmussen Jakob H.¹,Jorgensen Peter L.¹

Affiliation:

1. Biomembrane Research Center, August Krogh Institute, Copenhagen University, 2100 Copenhagen OE, Denmark

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi981898w

Reference45 articles.

1. Structural basis for E1–E2 conformational transitions in Na, K-pump and Ca-pump proteins

2. Occlusion of 22Na+ and 86Rb+ in membrane-bound and soluble protomeric alpha beta-units of Na,K-ATPase.

3. Extensive digestion of Na+,K(+)-ATPase by specific and nonspecific proteases with preservation of cation occlusion sites.

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