Glyceraldehyde-3-phosphate dehydrogenase from Ehrlich ascites carcinoma cells: Its possible role in the high glycolysis of malignant cells

European Journal of Biochemistry

Volumn 262, Issue 2, 1999, Pages 386-395

  Bagui, Swapna ^a   Ray, Manju ^a   Ray, Subhankar ^b  

^a DEPARTMENT OF MATERIALS SCIENCE   (India)

^b UNIVERSITY OF CALCUTTA   (India)

Author keywords

ATP; Glyceraldehyde 3 phosphate dehydrogenase; Malignancy

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; CANCER CELL; EHRLICH ASCITES TUMOR CELL; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; GLYCOLYSIS; MOUSE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN INTERACTION;

ADENOSINE TRIPHOSPHATE; ANIMALS; CARCINOMA, EHRLICH TUMOR; CHROMATOGRAPHY, ION EXCHANGE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; ENZYME STABILITY; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; GLYCOLYSIS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR WEIGHT; NAD; NADP; RABBITS; SUBSTRATE SPECIFICITY;

EID: 0033153230     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00384.x     Document Type: Article

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