Literature DB >> 139894

Ouabain-sensitive 42K binding to Na+, K+-ATPase purified from canine kidney outer medulla.

H Matsui, Y Hayashi, H Homareda, M Kimimura.   

Abstract

Entities:  

Mesh：

Substances：

Year:  1977        PMID： 139894     DOI： 10.1016/0006-291x(77)91052-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


× No keyword cloud information.
  7 in total

1.  Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis.

Authors:  G G Hammes
Journal:  Proc Natl Acad Sci U S A       Date:  1982-11       Impact factor: 11.205

2.  Characterization of conformational changes in (Na,K) ATPase labeled with fluorescein at the active site.

Authors:  S J Karlish
Journal:  J Bioenerg Biomembr       Date:  1980-08       Impact factor: 2.945

3.  Occlusion of rubidium ions by the sodium-potassium pump: its implications for the mechanism of potassium transport.

Authors:  I M Glynn; D E Richards
Journal:  J Physiol       Date:  1982-09       Impact factor: 5.182

Review 4.  Na+, K+-ATPase: relation of conformational transitions to function.

Authors:  A Askari
Journal:  Mol Cell Biochem       Date:  1982-04-02       Impact factor: 3.396

5.  Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour.

Authors:  J Jensen; J G Nørby; P Ottolenghi
Journal:  J Physiol       Date:  1984-01       Impact factor: 5.182

6.  Passive rubidium fluxes mediated by Na-K-ATPase reconstituted into phospholipid vesicles when ATP- and phosphate-free.

Authors:  S J Karlish; W D Stein
Journal:  J Physiol       Date:  1982-07       Impact factor: 5.182

7.  Multiple binding of thallium and rubidium to potassium-activated yeast aldehyde dehydrogenase. Influences on tertiary structure, stability and catalytic activity.

Authors:  K A Bostian; G F Betts; W K Man; M N Hughes
Journal:  Biochem J       Date:  1982-10-01       Impact factor: 3.857
  7 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.