ISSN:
1432-072X
Keywords:
Archaebacteria
;
Haloarcula vallismortis
;
Glyceraldehyde 3-phosphate dehydrogenase
;
Halophilism
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00258139
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