Purification and Immunochemical Characterization of NADP-Dependent Glyceraldehyde 3-Phosphate Dehydrogenase of Euglena gracilis |
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Authors: | Heide-Birgitt Theiss-Seuberling |
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Institution: | Institut f?r Allgemeine Botanik und Pflanzenphysiologie der Justus-Liebig-Universit?t Giessen Heinrich-Buff-Ring 54-62, D-6300 Giessen, Federal Republic of Germany |
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Abstract: | NADP-dependent glyceraldehyde 3-phosphate dehydrogenase fromEuglena gracilis (EC 1.2.1.13
EC]
) was purified about 170-fold bya two-step procedure involving DEAE-SH cellulose chromatographyand affinity chromatography on ADP-Sepharose. The homogeneousenzyme from mildly sonicated cells contained equal amounts oftwo types of subunits with mol wts of 34,000 (A) and 38,000(B). The active enzyme had a mol wt 144,000 and is thereforean A2B2 tetramer. Enzyme from strongly sonicated Euglena cellscontained, in addition, a second allomer with a probable A4structure. NADdependent glyceraldehyde 3-phosphate dehydrogenase,a tetramer with 36,000 mol wt subunits, was unrelated immunologicallyto the NADP-dependent enzyme although the latter also showedminor NAD-dependent activity. Both isoenzymes of the NADPlinkedglyceraldehyde 3-phosphate dehydrogenase, however, were immunologicallyidentical.
1Dedicated, to Prof. Dr. O. H. Volk on his 80th birthday. (Received October 13, 1982; Accepted March 21, 1984) |
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