
doi: 10.1007/bf01990378
pmid: 6641908
Porcine liver beta-D-glucose dehydrogenase has been isolated using Triton X-114 to release it from the endoplasmic reticulum. The purified enzyme contains a limited amount (1.7%) of lipid material, including cholesterol, fatty acids, mono and diglycerides, phosphatidylcholine, phosphatidylethanolamine, and cholesterol esters. This enzyme is a tetrameric protein containing an extensive number of hydrophobic residues. This form of glucose dehydrogenase is capable of turning over both beta-D-glucose and alpha-D-glucose-6-phosphate in vivo as indicated from a steady state kinetic analysis at 37 degrees C.
Male, Swine, Phosphatidylethanolamines, Glucose Dehydrogenases, Glucose 1-Dehydrogenase, Hydrogen-Ion Concentration, Endoplasmic Reticulum, Lipids, Substrate Specificity, Kinetics, Liver, Animals, Carbohydrate Dehydrogenases, Female, Amino Acids
Male, Swine, Phosphatidylethanolamines, Glucose Dehydrogenases, Glucose 1-Dehydrogenase, Hydrogen-Ion Concentration, Endoplasmic Reticulum, Lipids, Substrate Specificity, Kinetics, Liver, Animals, Carbohydrate Dehydrogenases, Female, Amino Acids
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