(Q67264313)

English

The K+-induced apparent heterogeneity of high-affinity nucleotide-binding sites in (Na+ + K+)-ATPase can only be due to the oligomeric structure of the enzyme

scientific article published on 01 January 1983

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11 September 2019

The K+-induced apparent heterogeneity of high-affinity nucleotide-binding sites in (Na+ + K+)-ATPase can only be due to the oligomeric structure of the enzyme (English)

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11 September 2019

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20 September 2023

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20 September 2023

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P. Ottolenghi

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20 September 2023

J. Jensen

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1 January 1983

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11 September 2019

5 January 1983

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National Center for Biotechnology Information

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=6297576

20 September 2023

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20 September 2023

https://api.elsevier.com/content/article/PII:0005273683903723?httpAccept=text/plain

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20 September 2023

Biochimica et Biophysica Acta

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11 September 2019

727

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11 September 2019

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11 September 2019

89-100

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11 September 2019

Purification and characterization of (Na+ plus K+ )-ATPase. IV. Estimation of the purity and of the molecular weight and polypeptide content per enzyme unit in preparations from the outer medulla of rabbit kidney

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A new proposal regarding the subunit composition of (Na+ + K+)ATPase

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Mutual exclusion of ATP, ADP and g-strophanthin binding to NaK-ATPase.

4

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Protein affinities for small molecules: Conceptions and misconceptions

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Purification and characterization of (Na+ plus K+ )-ATPase. 3. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate

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Effect of ATP on the intermediary steps of the reaction of the (Na+ plusK+)-dependent enzyme system. III. Effect on the p-nitrophenylphosphatase activity of the system.

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Protein measurement with the Folin phenol reagent

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Binding of ATP to brain microsomal ATPase. Determination of the ATP-binding capacity and the dissociation constant of the enzyme-ATP complex as a function of K+ concentration

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Stability and ligand sensitivity of (3H)ouabain binding to (Na+ + K+)ATPase

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The effect of anti-L on ouabain binding to sheep erythrocytes

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A graphic method for the determination and presentation of binding parameters in a complex system

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Binding of ATP to Na+, K+-ATPase

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The correlation between ouabain binding and potassium pump inhibition in human and sheep erythrocytes.

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(Na+ + K+) ATPase has one functioning phosphorylation site per α subunit

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Polypeptide molecular weights of the (Na+,K+)-ATPase from porcine kidney medulla

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Membrane enzyme systems. Molecular size determinations by radiation inactivation

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Ultrastructure of the sodium pump: Comparison of thin sectioning, negative staining, and freeze-fracture of purified, membrane-bound (Na+, K+)-ATPase

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Adenosine diphosphate binding to sodium-plus-potassium ion-dependent adenosine triphosphatase. The role of lipid in the nucleotide-potassium ion interplay

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Soluble and active renal Na,K-ATPase with maximum protein molecular mass 170,000 ± 9,000 daltons; formation of larger units by secondary aggregation

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Identifiers

10.1016/0005-2736(83)90372-3

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6297576%20AND%20SRC:MED&resulttype=core&format=json

11 September 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6297576%20AND%20SRC:MED&resulttype=core&format=json

11 September 2019

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