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Glycerol‐3‐phosphate dehydrogenase (EC 1.1.1.8) from Dunaliella tertiolecta . I. Purification and kinetic properties
Author(s) -
Haus M.,
Wegmann K.
Publication year - 1984
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1984.tb06063.x
Subject(s) - glycerol , dunaliella , dehydrogenase , chromatography , dihydroxyacetone phosphate , dihydroxyacetone , glycerol 3 phosphate dehydrogenase , chemistry , biochemistry , phosphate , sephadex , enzyme , affinity chromatography , osmotic shock , biology , algae , botany , gene
A rapid purification procedure for glycerol‐3‐phosphate dehydrogenase from Dunaliella tertiolecta (strain 19‐6 of the algal collection of the Univ. of Göttingen), the initial enzyme in the glycerol cycle, has been developed on the basis of affinity chromatography on Blue Sepharose and subsequent desalting by Sephadex G‐50. The achieved purification was 126‐fold. The pH optimum of dihydroxyacetone phosphate reduction is 7, that of glycerol‐3‐phosphate oxidation is about 9. The in vitro enzymatic activity obtained from cell extracts is higher than the required activity for the observed glycerol production rates under osmotic stress in vivo.