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Partial Purification and Characterization of UDP-Glucose-4-Epimerase from Solieria chordalis (Rhodophyceae)
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F. Goulard
Published/Copyright:
June 1, 2005
Abstract
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 μM and 630 μM, respectively.
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Published Online: 2005-06-01
Published in Print: 2003-01-27
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- To Our Authors, Readers and Subscribers
- Chamaebotrys erectus sp. nov. (Rhodymeniales, Rhodophyta) from the Socotra Archipelago, Yemen
- Photosynthetic Performance and Pigment Content of Different Developmental Stages of Ecklonia cava (Laminariales, Phaeophyceae)
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