PURIFICATION AND PROPERTIES OF 6-PHOSPHOGLUCONATE DEHYDROGENASE FROM BEET LEAVES

Authors
SIGNORINI M BREGOLI AM CASELLI L BERGAMINI CM
Citation
M. Signorini et al., PURIFICATION AND PROPERTIES OF 6-PHOSPHOGLUCONATE DEHYDROGENASE FROM BEET LEAVES, Biochemistry and molecular biology international, 35(3), 1995, pp. 669-675
Citations number
19
Categorie Soggetti
Biology
Journal title
Biochemistry and molecular biology international → ACNP
ISSN journal
10399712
Volume
35
Issue
3
Year of publication
1995
Pages
669 - 675
Database
ISI
SICI code
1039-9712(1995)35:3<669:PAPO6D>2.0.ZU;2-T
Abstract
We have purified to homogeneity 6-Phosphogluconate dehydrogenase from leaves of silver beet (Beta vulgaris L.) by means of cation-exchange a nd affinity chromatography. The enzyme is a homodimer of 52 kDa subuni ts; it catalyzes NADP dependent oxidation of 6-P-gluconate with Michae lian substrate saturation. The activity is affected by some intermedia tes of carbohydrate metabolism, particularly erythrose-4-P. Subcellula r fractionation studies indicate the cytosolic location of the enzyme.