Gastric H/K-ATPase Liberates Two Moles of Pi from One Mole of Phosphoenzyme Formed from a High-Affinity ATP Binding Site and One Mole of Enzyme-Bound ATP at the Low-Affinity Site during Cross-Talk between Catalytic Subunits-Reference-Cited by-同舟云学术

Gastric H/K-ATPase Liberates Two Moles of Pi from One Mole of Phosphoenzyme Formed from a High-Affinity ATP Binding Site and One Mole of Enzyme-Bound ATP at the Low-Affinity Site during Cross-Talk between Catalytic Subunits

Published:2002-01-25 Issue:7 Volume:41 Page:2438-2445
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Abe Kazuhiro¹,Kaya Shunji¹,Imagawa Toshiaki¹,Taniguchi Kazuya¹

Affiliation:

1. Biological Chemistry, Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi015622r

Reference42 articles.

1. Albers, R. W. (1976) inThe Enzymes of Biological Membranes(Martonossi, A., Ed.), Vol. 3, pp 283−301, Plenum Publishing Corp., New York.

2. Glynn, I. M. (1985) inThe Enzymes of Biological Membranes(Martonossi, A., Ed.), Vol. 3, pp 35−114, Plenum Publishing Corp., New York.

3. OCCLUDED CATIONS IN ACTIVE TRANSPORT

4. Structural organization, ion transport, and energy transduction of P-type ATPases

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