scholarly journals The oxidative pathway of carbohydrate metabolism in Escherichia coli. 3. Glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in cells grown under different conditions*

1956 ◽  
Vol 63 (4) ◽  
pp. 587-593 ◽  
Author(s):  
Dwight B. McNair Scott
1980 ◽  
Vol 84 (3) ◽  
pp. 467-471
Author(s):  
N. DESHPANDE ◽  
IRENE MITCHELL

The effects of administration of testosterone propionate on the activities of seven of the enzymes of carbohydrate metabolism in normal rat mammary glands were investigated and the validity of the results was confirmed by simultaneous injection of the hormone and cyproterone acetate. The administration of the androgen increased the activities of phosphofructokinase (PFK), glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH) and lactate dehydrogenase (LDH) in glands from both intact and from ovariectomized and adrenalectomized animals. Administration of cyproterone acetate alone resulted in a significant reduction in the activities of PFK and G6PDH and when given together with the androgen it inhibited increases in the activities of PFK, G6PDH, 6PGDH and LDH induced by testosterone. It was concluded that these results did not explain the known inhibitory effects of the androgen on normal mammary gland growth and function.


1976 ◽  
Vol 35 (3) ◽  
pp. 407-411 ◽  
Author(s):  
J. Pearce ◽  
E. F. Unsworth

1. Feeding sheep a concentrate diet compared with grass diets increased the hepatic specific activities of the three glycolytic enzymes studied, and that of glucose-6-phosphate dehydrogenase (EC 1.1.1.49), and reduced the specific activity of D-fructose-1,6-diphosphate 1-phosphohydrolase (EC 3.1.3.11). The specific activities of phosphogluconate dehydrogenase (EC 1.1.1.43) and malate dehydrogenase (decarboxylating) (NADP) (EC 1.1.1.40) were unaffected by diet.


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