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However, examination of the normal and variant enzymes under simulated physiologic conditions, with the effects of various intermediate metabolites and coenzymes in red cells being taken into consideration, reveal that the G6PD's from hemolytic variant subjects are strongly inhibited by a physiologic concentration of NADPH because of their high Michaelis constant for NADP or low inhibition constant for NADPH, and they are more sensitive to inhibition by ATP. These variant enzymes cannot generate enough NADPH in red cells to maintain an adequate concentration of reduced glutathione. The nonhemolytic variant enzymes are far less sensitive to the inhibition by NADPH because of their low Michaelis constant for NADP and high inhibition constant for NADPH. The physiologic activity of these nonhemolytic variant enzymes is estimated to be more than 30 percent of the activity of the normal G6PD, and this activity is adequate to maintain the red cells unhemolyzed.<\/jats:p>","DOI":"10.1126\/science.179.4073.532","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T14:05:45Z","timestamp":1160057145000},"page":"532-537","source":"Crossref","is-referenced-by-count":196,"title":["Hemolytic Anemia and G6PD Deficiency"],"prefix":"10.1126","volume":"179","author":[{"given":"Akira","family":"Yoshida","sequence":"first","affiliation":[{"name":"Department of biochemical genetics, City of Hope National Medical Center, Duarte, California 91010"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"221","reference":[{"key":"e_1_2_1_1_1","unstructured":"World Health Organization Technical Report 336 (1967)."},{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1021\/bi00779a009","volume":"10","year":"1971","unstructured":"AFOLAYAN, A, GENETIC VARIANTS OF HUMAN ERYTHROCYTE GLUCOSE 6-PHOSPHATE DEHYDROGENASE .1. 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