Electrophoretic Heterogeneity of Glucose-6-Phosphate Dehydrogen Ase and Its Relationship to Enzyme Deficiency in Man

Abstract

33 Kurland and Maal0e3E postulate that the effect is due to a constant small turnover of proteins. In the presence of chloramphenicol the degradation would be unimpaired, but since the rebuilding of proteins is stopped, the amino acid pool would be replenished. For this idea experimental evidence is given; indeed they showed that in bacteria which had been starved for the required amino acid, the RNA synthesis initiated by chloramphenicol recovers later than in that case where both an amino acid and chloramphenicol were used. However, in the latter case, a similar but shorter lag was also observed. They showed also that small concentrations of chloramphenicol are not effective to initiate the recovery in absence of the amino acid. In our experiments with vegetative phage DNA, we found no such lag, although the infective cells had been starved for 10-15 min. (We have also observed similar stringency and lack of a lag in phage infected bacteria starved for only 5 min.) 34Bendich, A., personal communication.

Evidence for four types of erythrocyte glucose-6-phosphate dehydrogenase from G-6-PD-deficient human subjects.

“…Kirkman and associates have reported patients with CNSHA with G-6-PD electrophoretic mobility similar to normal Caucasians, type B ( 18,19). The patient designated "Eysson" by Boyer and colleagues (16) showed a slower mobility than type B. Obviously, comparative studies of these more unusual deficient patients should be carried out.…”

“…Characterization of the erythrocyte G-6-PD from normal and drug-sensitive male Negro patients has been reported (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). The enzyme from the drug-sensitive Negro male was indistinguishable from that of normal Negro males with respect to substrate and inhibitor affinity, pH optimum, and general stability (7).…”

Glucose-6-phosphate dehydrogenase deficiency: a historical perspective

“…Thus, it was initially assumed that G6PD deficiency was a single disorder, but the studies of Marks and Gross 43 showed that G6PD deficiency in Mediterranean peoples was much more severe than among African-Americans. With the development of electrophoretic methods for measuring the mobility of the enzyme on starch gel 44 and for studying the kinetic properties of the residual enzyme, 45 much greater heterogeneity became apparent. These methods were standardized by an expert committee convened by the World Health Organization (WHO), and these standard methods were used by most investigators.…”

G6PD Deficiency in an HIV Clinic Setting in the Dominican Republic

“…Of 55 patients sequenced, 29 carried at least one G6PD A− allele (i.e., containing the nonpathogenic A376G and pathogenic G202A substitutions). The G6PD A+ allele (A376G alone), exhibiting normal enzymatic activity, 30 was the only other variant detected. All biochemically deficient males were hemizygous for the A− variant; all biochemically deficient females were heterozygotes, except for one homozygous deficient female, whose enzyme level resembled that of male hemizygotes.…”