ZIB

Treffer pro Seite

Treffer 1 - 1 | 1 Treffer

Sortierung

Digitale Medien

Characterization of the glyceraldehyde 3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis (1993)

Prüß, Birgit ; Meyer, Helmut E. ; Holldorf, August W.

Springer

Archives of microbiology 160 (1993), S. 5-11

zur Merkliste hinzufügen auf der Merkliste

Details

ISSN: 1432-072X

Schlagwort(e): Archaebacteria ; Haloarcula vallismortis ; Glyceraldehyde 3-phosphate dehydrogenase ; Halophilism

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: 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.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00258139

Permalink

Bibliothek	Standort	Signatur	Band/Heft/Jahr	Verfügbarkeit

Andere fanden auch interessant ...

Artikel (Nationallizenzen)

Volltext

Treffer 1 - 1 | 1 Treffer