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G6PD Varadero A New Variant of Glucose‐6‐Phosphate Dehydrogenase Associated with Congenital Nonspherocytic Hemolytic Anemia
Author(s) -
Estrada M.,
García M.,
Gutiérrez A.,
Quintero I.,
González R.
Publication year - 1982
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1982.tb01078.x
Subject(s) - glucose 6 phosphate dehydrogenase , dehydrogenase , nicotinamide adenine dinucleotide phosphate , phosphate , hemolytic anemia , chemistry , biochemistry , anemia , enzyme , nicotinamide adenine dinucleotide , chromatography , nad+ kinase , medicine , oxidase test
A glucose‐6‐phosphate dehydrogenase (G6PD) variant was studied in a mulatto patient with chronic nonspherocytic hemolytic anemia. This variant has reduced activity, increased thermolability, a reduced Michaelis constant for glucose‐6‐phosphate, slightly increased electrophoretic mobility, a biphasic pH activity profile, high 2‐deoxy‐glucose‐6‐phosphate utilization, normal diamino nicotinamide adenine dinucleotide phosphate utilization and a peak of elution profile after G6PD B. The electrophoretic, kinetic, and chromatographic properties of this erythrocyte G6PD variant allow the conclusion that G6PD Varadero is probably a new variant.