An ATP-modulated specific association of glyceraldehyde-3-phosphate dehydrogenase with human erythrocyte glucose transporter.

Association of glyceraldehyde 3-phosphate dehydrogenase with the human erythrocyte membrane. Effect of detergents, trypsin, and adenosine triphosphate.

Glyceraldehyde 3-phosphate dehydrogenase is one of the major protein components associated with the erythrocyte membrane. This has been shown by activity studies of specific membrane extracts and by the specificity of iodoacetate inactivation and labeling of the enzyme. Studies on the association of the enzyme with the membrane are complicated by the tendency of the ghosts to seal under certain...

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

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...

Erythrocyte glucose 6-phosphate dehydrogenase of normal and mutant human subjects: properties of the purified enzymes.

A deficiency in human erythrocyte glucose 6-phosphate dehydrogenase may be genetically determined (l-4) or occur in normal erythrocytes as they age in tivo (5, 6). The inherited glucose-6-P dehydrogenase deficiency, which is associated with hemolytic anemia upon exposure to a variety of agents, affords an opportunity in man to study further the mechanisms by which genes can lead to a decrease i...

Characterization of Glycolytic Enzyme Interactions with Murine Erythrocyte Membranes in Wild type and Membrane Protein Knockout Mice Short title for the running head: GLYCOLYTIC ENZYME INTERACTIONS WITH ERYTHROCYTE MEMBRANES

Previous research has shown that glycolytic enzymes (GEs) exist as multi-enzyme complexes on the inner surface of human erythrocyte membranes. Because GE binding sites have been mapped to sequences on the membrane protein, band 3, that are not conserved in other mammalian homologs, the question arose whether GEs can organize into complexes on other mammalian erythrocyte membranes. To address th...