Stimulation of glyceraldehyde-3-phosphate dehydrogenase by oxyhemoglobin.

Abstract:

:Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme regulated by many diverse mechanisms. In this study we present evidence that GAPDH activity is stimulated in the presence of oxyhemoglobin (2.3-fold, P < 0.005). No stimulation was seen by myoglobin, and only slight stimulation (1.2-fold, not significant) by methemoglobin was observed. Such stimulation may have physiological significance as 1,3-bis-phosphoglycerate, the product of GAPDH, isomerises to 2,3-bis-phosphoglycerate, an allosteric effector that decreases the oxygen affinity of hemoglobin, thus providing a feedback loop. The results suggest that when assaying GAPDH activity in biological samples, hemoglobin content should be taken into account.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Brookes PS,Land JM,Clark JB,Heales SJ

doi

10.1016/s0014-5793(97)01181-2

subject

Has Abstract

pub_date

1997-10-13 00:00:00

pages

90-2

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)01181-2

journal_volume

416

pub_type

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