Multiple molecular forms of lactate dehydrogenase and glucose 6-phosphate dehydrogenase in normal and abnormal human breast tissues.
Normal and abnormal breast samples of women were analyzed for multiple molecular forms of lactate dehydrogenase and glucose 6-phosphate dehydrogenase, using acrylamide disc gel electrophoresis and specific enzyme staining techniques for separation and quantitation. Infiltrating ductal carcinomas demonstrated a significant increase (three to six-fold) in the proportion of LDH-5 compared to samples of normal breast, fibrocystic disease and fibroadenoma, indicative of a shift toward the muscle-type lactate dehydrogenase in neoplasia. For glucose 6-phosphate dehydrogenase, carcinomas were found to contain increased proportions of the fastest migrating species, G6PD-I. Total enzyme activity/mg DNA was elevated in meoplastic tissues. Little or no alteration in isoenzyme profiles could be related to menopausal status of the patient.
D001940:Breast / Q000201:enzymology*; D001941:Breast Diseases / Q000201:enzymology*; D001943:Breast Neoplasms / Q000201:enzymology*; D002285:Carcinoma, Intraductal, Noninfiltrating / Q000201:enzymology; D004247:DNA / Q000032:analysis; D005260:Female; D005954:Glucosephosphate Dehydrogenase / Q000032:analysis*; D006801:Humans; D007527:Isoenzymes / Q000032:analysis*; D007770:L-Lactate Dehydrogenase / Q000032:analysis*; D008593:Menopause
D007527:Isoenzymes; D004247:DNA; D007770:L-Lactate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase