F. Goulard, P. Pondaven, M. Diouris, E. Deslandes, J. Y. Floch
Partial Purification and Characterization of UDP-Glucose-4-Epimerase from Solieria chordalis (Rhodophyceae)
The partial purification of UDP-glucose-4-epimerase was carried out on the red macroalga Solieria chordalis. A 60-fold purification factor was obtained by chromatography on DEAE Protein-Pack 8 HR and Superose 12. Gel-filtration fast protein liquid chromatography (FPLC) showed that the enzyme had an apparent molecular mass of 130 kDa. The UDP-glucose-4-epimerase from Solieria chordalis does not require complementary NAD addition for activity, unlike the enzyme from some other organisms. Moreover, the optimal pH was at 8.5 and the apparent KM values for UDP-glucose and UDP-galactose were 87 ?M and 630 ?M, respectively.
Botanica Marina, Walter de Gruyter
Print ISSN: 0006-8055
Volume: 46, 01/2003
Pages: 107 - 111
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