Maleimide as an inhibitor in measurement of erythrocyte glucose-6-phosphate dehydrogenase activity.

INHIBITION OF HUMAN ERYTHROCYTE GLUCOSE 6-PHOSPHATE DEHYDROGENASE ACTIVITY BY DEHYDROEPIANDROSTERONE AND RELATED STEROIDS.

The inhibitory effects of several steroids on G6PD activity using intact erythrocytes are reported. Incubation of whole blood with dehydroepiandrosterone (DHEA) resulted in 42% and 12% inhibition in the enzyme activity in the presence and absence of oxygen, respectively. Addition of epinephrine and/or aminophylline into the incubation medium caused further enzyme inhibition suggesting a po...

Inhibition of Human Erythrocyte Glucose 6-Phosphate Dehydrogenase by Cadmium, Nickel and Aluminium

P-90: Effect of Phosphodiesterase Type3 Inhibitor, Cilostamide, on The Developmental Competence of Ovine OocytesIsolated by Glucose 6-Phosphate Dehydrogenase Activity

Background: The developmental competence of oocytes matured in vitro (IVM) is yet far below than in vivo counterparts. Recent studies suggest that the asynchrony between nuclear/cytoplasmic maturation and the initial low/heterogeneous quality of oocytes are the most important factors affecting IVM success. We investigated whether selection of growing oocytes (based on their glucose 6- phosphate...

Measurement of erythrocyte glucose-6-phosphate dehydrogenase activity using a centrifugal analyzer.

We describe two improved methods for determination of erythrocyte glucose-6-phosphate dehydrogenase activity. One method is an “enzyme-linked” procedure in which an excess of 6-phosphogluconate dehydrogenase is used to produce two moles of NADPHfor each mole of glucose-6-phosphate oxidized. In the other method 2,3-diphosphoglycerate is used to inhibit the variable contribution of endogenous 6-p...

REASSOCIATION AND REACTIVATION OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM STREPTOMYCES AUREOFACIENS AFTER DENATURATION BY 6 M UREA

Glucose 6-phosphate dehydrogenase (G6PD) from Streptomyces aureofaciens was purified and denatured in 6 M urea. Denaturation led to complete dissociation of the enzyme into its inactive monomers, 98% loss of the enzyme activity, about 30% decrease in the protein fluorescence and a 10 nm red shift in the emission maximum. Dilution of urea-denatured enzyme resulted in regaining of the enzyme acti...