Abstract
SHAW and Barto1 have demonstrated the presence of an autosomally inherited glucose-6-P dehydrogenase (G6PD) in the deer mouse. Subsequently, Ohno et al.2 found a similar enzyme in trout and showed that this enzyme and the autosomally inherited mouse enzyme differed from the sex-linked G6PD in possessing marked catalytic activity with galactose-6-P. This autosomally inherited G6PD was therefore named hexose-6-P dehydrogenase (H6PD)2,3. It was shown to oxidize glucose-6-P, galactose-6-P, mannose-6-P, and 2-deoxy glucose-6-P with a Km of the order of 10−5 M. It also oxidizes glucose with a Km of 0.7 M3. It appears to be identical to the so-called “glucose dehydrogenase”. The enzyme utilizes both NAD and NADP and is microsome-bound. G6PD is localized in the soluble fraction of the cells of various tissues. Although it has been shown that two dehydrogenases from liver have different substrate specificity, molecular weight and elec-trophoretic mobility3,4, it has been suggested that the two enzymes are merely isozymes and they might be interconvertible5–7. We have now partially purified the two enzymes from human liver and show that they have different immunological properties.
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References
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SRIVASTAVA, S., BLUME, K., BEUTLER, E. et al. Immunological Difference between Glucose-6-P Dehydrogenase and Hexose-6-P Dehydrogenase from Human Liver. Nature New Biology 238, 240–241 (1972). https://doi.org/10.1038/newbio238240a0
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DOI: https://doi.org/10.1038/newbio238240a0
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