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Title: Inhibition of glycolysis by H sub 2 O sub 2 is not due to inhibition of G3PDH

Conference · · FASEB Journal (Federation of American Societies for Experimental Biology); (United States)
OSTI ID:6053816
;  [1]
  1. Oakland Univ., Rochester, MI (United States)

The inhibition of glycolysis by H{sub 2}O{sub 2} has been attributed to oxidative inactivation of glyceraldehyde-3-phosphate dehydrogenase (G3PDH). The authors previous work using isolated, intact rat retinas suggested that the inter-action between H{sub 2}O{sub 2} and pyruvate could also contribute to the decrease in glycolysis, though G3PDH was not measured. The strategy of the present work was to compare the effects of H{sub 2}O{sub 2} with those of iodoacetate (IAA), which inactivates G3PDH but does not interact with pyruvate, on glycolysis of retinas and on the activity of G3PDH, as measured in post-incubation supernatant fractions of these retinas. When the enzyme activity was inhibited by 50% with 0.01 mM IAA, the glycolytic rate was not significantly different from the control value. However, when H{sub 2}O{sub 2} produced a 50% inhibition of the enzyme the glycolytic rate was decreased by 70% relative to the control tissue. With 0.1 mM H{sub 2}O{sub 2}, the enzyme inhibition was about 15% but the lactate produced declined by about 20%. Glycolysis was suppressed completely when the enzyme was inhibited by 99+% with either H{sub 2}O{sub 2} or IAA. Though G3PDH is clearly inhibited by H{sub 2}O{sub 2}, it appears that this inhibition alone may not account for the decline in glycolysis.

OSTI ID:
6053816
Report Number(s):
CONF-9104107-; CODEN: FAJOE
Journal Information:
FASEB Journal (Federation of American Societies for Experimental Biology); (United States), Vol. 4:3; Conference: 75. annual meeting of the Federation of American Societies for Experimental Biology (FASEB), Atlanta, GA (United States), 21-25 Apr 1991; ISSN 0892-6638
Country of Publication:
United States
Language:
English