Interaction between aldolase and vacuolar H+-ATPase. Evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump

Journal of Biological Chemistry

Volumn 276, Issue 32, 2001, Pages 30407-30413

  Lu, Ming ^a   Holliday, L Shannon ^a   Zhang, Li ^a   Dunn Jr , William A ^a   Gluck, Stephen L ^a  

^a UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BIOASSAY; BIOLOGICAL MEMBRANES; CELL CULTURE; CLONING; HYDROLYSIS; IMMUNOLOGY; PROTONS;

IMMUNOCYTOCHEMICAL ASSAYS; PLASMA MEMBRANES;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATE; CHIMERIC PROTEIN; COMPLEMENTARY DNA; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MONOCLONAL ANTIBODY; PROTON; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; FRUCTOSE; GLUCOSE 6 PHOSPHATE ISOMERASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME REGULATION; ENZYME SUBSTRATE; ENZYME SUBUNIT; GLYCOLYSIS; HEREDITARY FRUCTOSE INTOLERANCE; KIDNEY EPITHELIUM; KIDNEY MICROSOME; KIDNEY PROXIMAL TUBULE; MOUSE; NONHUMAN; OSTEOCLAST; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; URINE ACIDIFICATION; YEAST CELL; ANIMAL; BINDING SITE; CATTLE; CELL MEMBRANE; CELL NUCLEUS; ENZYMOLOGY; GENETICS; HUMAN; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; KIDNEY; METABOLISM; MICROSOME; MUTATION; PLASMID; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SERODIAGNOSIS; TWO HYBRID SYSTEM;

ANIMALIA; BOVINAE;

ANIMALS; BINDING SITES; CATTLE; CELL MEMBRANE; CELL NUCLEUS; DNA, COMPLEMENTARY; FRUCTOSE; FRUCTOSE-BISPHOSPHATE ALDOLASE; GLUCOSE-6-PHOSPHATE ISOMERASE; GLUTATHIONE TRANSFERASE; HUMANS; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; KIDNEY; MICROSOMES; MUTATION; OSTEOCLASTS; PLASMIDS; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTON-TRANSLOCATING ATPASES; PROTONS; TWO-HYBRID SYSTEM TECHNIQUES; VACUOLAR PROTON-TRANSLOCATING ATPASES;

EID: 0035839499     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M008768200     Document Type: Article

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