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Volumn 41, Issue 7, 2002, Pages 2438-2445
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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
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Author keywords
[No Author keywords available]
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Indexed keywords
LOW-AFFINITY;
CATALYSIS;
CONCENTRATION (PROCESS);
HYDROLYSIS;
MAGNESIUM PRINTING PLATES;
PHOSPHORUS;
RATE CONSTANTS;
ENZYMES;
ADENOSINE TRIPHOSPHATASE;
ADENOSINE TRIPHOSPHATE;
HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE;
PHOSPHATE;
ANIMAL CELL;
ARTICLE;
BINDING AFFINITY;
BINDING SITE;
CATALYSIS;
CONTROLLED STUDY;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME METABOLISM;
HYDROLYSIS;
NONHUMAN;
PHOSPHORYLATION;
PRIORITY JOURNAL;
PROTEIN BINDING;
ADENOSINE TRIPHOSPHATE;
ANIMALS;
BINDING SITES;
CATALYTIC DOMAIN;
COLD;
H(+)-K(+)-EXCHANGING ATPASE;
HEAT;
HYDROGEN-ION CONCENTRATION;
HYDROLYSIS;
MAGNESIUM;
PHOSPHATES;
PHOSPHOPROTEINS;
PHOSPHORUS RADIOISOTOPES;
PROTON-TRANSLOCATING ATPASES;
SWINE;
TRICHLOROACETIC ACID;
ANIMALIA;
SUS SCROFA;
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EID: 0037133301
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi015622r Document Type: Article |
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Times cited : (16)
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References (41)
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