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 Lettjournal_title
FEBS lettersauthors
Brookes PS,Land JM,Clark JB,Heales SJdoi
10.1016/s0014-5793(97)01181-2subject
Has Abstractpub_date
1997-10-13 00:00:00pages
90-2issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(97)01181-2journal_volume
416pub_type
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