Intramembraneous localization of rat liver microsomal hexose-6-phosphate dehydrogenase and membrane permeability to its substrates.
A method for purifying hexose-6-phosphate dehydrogenase (beta-D-glucose: NAD(P) -oxidoreductase, EC 1.1.1.47) from rat liver microsomes is described. The purified enzyme was shown to be homogeneous by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. It is shown that the enzyme is bound to the inner surface of microsomal membranes, and that glucose 6-phosphate, but not NADP, penetrates almost freely into the membranes at 37 degrees C.
D000818:Animals; D000937:Antigen-Antibody Reactions; D001692:Biological Transport; D002237:Carbohydrate Dehydrogenases / Q000032:analysis*; D005948:Glucose Dehydrogenases / Q000032:analysis* / Q000302:isolation & purification; D005958:Glucosephosphates / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008563:Membrane Lipids / Q000502:physiology; D008566:Membranes / Q000201:enzymology; D008862:Microsomes, Liver / Q000201:enzymology*; D009249:NADP / Q000378:metabolism; D010539:Permeability; D051381:Rats; D013050:Spectrometry, Fluorescence
D005958:Glucosephosphates; D008563:Membrane Lipids; D009249:NADP; D002237:Carbohydrate Dehydrogenases; D005948:Glucose Dehydrogenases