Abstract
The A(-) type of glucose 6-phosphate dehydrogenase (EC 1.1.1.49) has been isolated from human erythrocytes deficient in this enzyme. The specific activity of the purified protein is similar to that previously reported for the enzyme isolated from normal, nondeficient erythrocytes. During the purification procedure, a portion of the A(-) enzyme converts spontaneously, from the native "fraction I", to a "fraction II" having different kinetic and chromatographic properties. The conversion of fraction I to II can be reproduced freely by treatment with iodosobenzoate, and fraction II can be converted back to fraction I by treatment with dithioglycol. We suggest that fraction II is an enzyme species in which one or more sulfhydryl groups have been oxidized to disulfide(s). The tendency to oxidation appears to be a property specific to the A(-) variant and may represent the basis for its rapid rate of inactivation and consequent deficiency in vivo.
MeSH Terms
Blood Protein Electrophoresis
Centrifugation, Density Gradient
Chromatography, Gel
Disulfides/biosynthesis
Electrophoresis, Starch Gel
Enzyme Activation
Erythrocytes/enzymology
Genetic Variation
Glucosephosphate Dehydrogenase/blood,isolation & purification
Humans
Kinetics
Models, Structural
Molecular Biology
Oxidation-Reduction
Protein Conformation
Sulfhydryl Compounds/metabolism
Temperature
Chemicals
Disulfides
Sulfhydryl Compounds
Glucosephosphate Dehydrogenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Babalola O
Cancedda R
Luzzatto L
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24 references, click to expand
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