The molecular size required varies according to the reaction step round the sodium pump cycle (Q47188297)

11 January 2018

title

The molecular size required varies according to the reaction step round the sodium pump cycle (English)

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11 January 2018

author name string

Cavieres JD

series ordinal

1

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11 January 2018

language of work or name

English

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publication date

1 December 1987

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11 January 2018

published in

FEBS Letters

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11 January 2018

volume

225

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11 January 2018

issue

1-2

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11 January 2018

page(s)

145-150

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11 January 2018

https://api.crossref.org/works/10.1016%2F0014-5793%2887%2981147-X

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Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA.

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Membrane enzyme systems. Molecular size determinations by radiation inactivation

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Studies on (K+ + H+)-ATPase. VI. Determination on the molecular size by radiation inactivation analysis

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The interaction of potassium ions and ATP on the sodium pump of resealed red cell ghosts.

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Molecular weight determinations from radiation inactivation

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Calmodulin and the target size of the (Ca2+ + Mg2+)-ATPase of human red-cell ghosts

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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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ATP binding to solubilized (Na+ + K+)-ATPase. The abolition of subunit-subunit interaction and the maximum weight of the nucleotide-binding unit

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The interaction of ATP-analogues possessing a blocked gamma-phosphate group with the sodium pump in human red cells

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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Mechanism of the Na+, K+ pump protein structure and conformations of the pure

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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

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

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Soluble and enzymatically stable (Na+ + K+)-ATPase from mammalian kidney consisting predominantly of protomer alpha beta-units. Preparation, assay and reconstitution of active Na+, K+ transport

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Statistical estimations in enzyme kinetics

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10.1016/0014-5793(87)81147-X

21 January 2018

Identifiers

DOI

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11 January 2018

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11 January 2018