Purification and properties of 6-phosphogluconate dehydrogenase from beet leaves.
We have purified to homogeneity 6-Phosphogluconate dehydrogenase from leaves of silver beet (Beta vulgaris L.) by means of cation-exchange and affinity chromatography. The enzyme is a homodimer of 52 kDa subunits; it catalyzes NADP dependent oxidation of 6-P-gluconate with Michaelian substrate saturation. The activity is affected by some intermediates of carbohydrate metabolism, particularly erythrose-4-P. Subcellular fractionation studies indicate the cytosolic location of the enzyme.
Signorini
M
M
Dipartimento di Biochimica e Biologia Molecolare della Università di Ferrara, Italy.
Bregoli
A M
AM
Caselli
L
L
Bergamini
C M
CM
D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D005942:Gluconates / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009249:NADP / Q000494:pharmacology; D010084:Oxidation-Reduction; D010734:Phosphogluconate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013403:Sugar Phosphates / Q000494:pharmacology; D014675:Vegetables / Q000201:enzymology*
D005942:Gluconates; D046911:Macromolecular Substances; D013403:Sugar Phosphates; D009249:NADP; C026959:erythrose 4-phosphate; D010734:Phosphogluconate Dehydrogenase; C008884:6-phosphogluconic acid