In vitro growing human lymphocytes (HL) and fibroblasts, isolated from glucose-6-phosphate dehydrogenase (G6PD)-deficient subjects (Mediterranean variant), show a sharp decrease in this enzymatic activity and in NADPH:NADP+ ratio. These cells are less able than controls to hydroxylate benzo(a)pyrene
Effect of polyamines and palmitoyl-coenzyme A on glucose-6-phosphate dehydrogenase from the hepatopancreas of the sea musselMytilus edulis L
โ Scribed by Rodriguez-Torres, A. M. ;Villamarin, A. ;Ramos-Martinez, J. I.
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 495 KB
- Volume
- 249
- Category
- Article
- ISSN
- 0022-104X
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โฆ Synopsis
Aliphatic polyamines are able to relieve the inhibition of glucose-6-phosphate dehydrogenase (GGPDH) by palmitoyl-coenzyme A (CoA). Of the polyamines assayed, spermine was the most effective in relieving this inhibition, followed by spermidine and ethylenediamine. These data suggest that the extent of the ability to relieve the inhibition depends on the number of amino groups in the polyamine.
The polyamines act specifically on palmitoyl-CoA to free G6PDH from the inhibition by acyl-CoA. Polyamines also decrease the inhibition of GGPDH by NADPH. The combination of these two effects results in an observed increase in GGPDH activity.
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