Lens aldo-keto reductase of Camelus dromedarius: purification and properties.
Biochim Biophys Acta
; 993(1): 116-20, 1989 Oct 13.
Article
en En
| MEDLINE
| ID: mdl-2679888
ABSTRACT
Aldo-keto reductase has been purified 13,000-fold from the lens of the camel (Camelus dromedarius) to a specific activity of 85 U/mg protein. The enzyme is a monomeric protein, exhibiting a Mr = 40,000 upon polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. Camel lens aldo-keto reductase shows a broad substrate specificity, which is strictly dependent on NADPH, and is insensitive to inhibition by Sorbinil and valproate. Aldoses with a carbon chain with more than four residues, as well as glucuronate, are not reduced by the enzyme. On the basis of substrate specificity and sensitivity to inhibition, camel lens aldo-keto reductase appears to be distinct from the so far described aldose, aldehyde and carbonyl reductases.
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Banco de datos:
MEDLINE
Asunto principal:
Oxidorreductasas de Alcohol
/
Cristalino
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1989
Tipo del documento:
Article
País de afiliación:
Italia