Characterization of the glyceraldehyde 3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis |
| |
Authors: | Birgit Prüß Helmut E Meyer August W Holldorf |
| |
Institution: | (1) Institut für Physiologische Chemie, Ruhr-Universität Bochum, Universitätsstrasse 150, W-4630 Bochum, Germany |
| |
Abstract: | Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) from the extremely halophilic archaebacterium Haloarcula vallismortis has been purified in a four step procedure to electrophoretic homogeneity. The enzyme is a tetramer with a relative molecular mass of 160000. It is strictly NAD+-dependent and exhibits its highest activity in 2 mol/l KCl at 45°C. Amino acid analysis and isoelectric focusing indicate an excess of acidic amino acids. Two parts of the primary sequence are reported. These peptides have been compared with glyceraldehyde 3-phosphate dehydrogenases from other archaebacteria, eubacteria and eucaryotes. The peptides show a high grade of similarity to glyceraldehyde 3-phosphate dehydrogenase from eucaryotes.Abbreviations BCA
bicinchoninic acid
- CTAB
cetyltrimethyl ammonium bromide
- DTE
dithioerythritol
- DTT
dithiothreitol
- GAP
glyccraldehyde 3-phosphate
- GAPDH
glyceraldehyde 3-phosphate dehydrogenase |
| |
Keywords: | Archaebacteria Haloarcula vallismortis Glyceraldehyde 3-phosphate dehydrogenase Halophilism |
本文献已被 SpringerLink 等数据库收录! |