Inactivation of Na,K-ATPase following Co(NH3)4ATP binding at a low affinity site in the protomeric enzyme unit.

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The amino acid sequence 442GDASE446 in Na/K-ATPase is an important motif in forming the high and low affinity ATP binding pockets.

P2860

Q44605200-89F3D348-DC7A-4394-9B3D-37040C3A3F88

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Inactivation of Na,K-ATPase following Co(NH3)4ATP binding at a low affinity site in the protomeric enzyme unit.

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http://www.wikidata.org/entity/Q44319473

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2003 nî lūn-bûn

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name

Inactivation of Na,K-ATPase fo ...... in the protomeric enzyme unit.

@en

Inactivation of Na,K-ATPase fo ...... in the protomeric enzyme unit.

@nl

type

Item

label

Inactivation of Na,K-ATPase fo ...... in the protomeric enzyme unit.

@en

Inactivation of Na,K-ATPase fo ...... in the protomeric enzyme unit.

@nl

prefLabel

Inactivation of Na,K-ATPase fo ...... in the protomeric enzyme unit.

@en

Inactivation of Na,K-ATPase fo ...... in the protomeric enzyme unit.

@nl

P1476

Inactivation of Na,K-ATPase fo ...... in the protomeric enzyme unit.

@en

P2093

José D Cavieres

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P2860

Measurement of protein using bicinchoninic acid

Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution

Biochemistry of Na,K-ATPase.

The active site structure of Na+/K+-transporting ATPase: location of the 5'-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides released by trypsin.

Solubilized alpha beta Na,K-ATPase remains protomeric during turnover yet shows apparent negative cooperativity toward ATP

An evaluation of active enzyme centrifugation as a zonal and boundary technique by the analysis of simulated data.

Replacement of several single amino acid side chains exposed to the inside of the ATP-binding pocket induces different extents of affinity change in the high and low affinity ATP-binding sites of rat Na/K-ATPase.

Purification and characterization of (Na+, K+)-ATPase. V. Conformational changes in the enzyme Transitions between the Na-form and the K-form studied with tryptic digestion as a tool.

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

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.

P304

14688-14697

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scholarly article

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10.1074/JBC.M211128200

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English

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P478

278

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P50

Douglas G. Ward

P577

2003-02-18T00:00:00Z

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P698

12591931

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Inactivation of Na,K-ATPase following Co(NH3)4ATP binding at a low affinity site in the protomeric enzyme unit.

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P2860

P2860

Inactivation of Na,K-ATPase following Co(NH3)4ATP binding at a low affinity site in the protomeric enzyme unit.

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type

label

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698