The proteolytic nature of commercial samples of galactose oxidase. Purification of the enzyme by a simple affinity method.
Biochim Biophys Acta
; 438(2): 339-46, 1976 Jul 08.
Article
em En
| MEDLINE
| ID: mdl-952937
ABSTRACT
Several commercially available samples of galactose oxidase (D-galactose oxygen 6-oxidoreductase, EC 1.1.3.9) were found to contain high proteolytic activity on proteins such as fibrinogen, transferrin, albumin and casein. A simple, efficient method was devised for the purification of galactose oxidase which relies on the affinity of the enzyme for agarose (Sepharose 6B). The purified galactose oxidase was recovered in high yield free from proteolytic activity. The enzymic affinity for Sepharose and Sephadex was investigated to clarify the absorption mechanism.
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Base de dados:
MEDLINE
Assunto principal:
Peptídeo Hidrolases
/
Oxirredutases do Álcool
/
Galactose Oxidase
Tipo de estudo:
Diagnostic_studies
/
Evaluation_studies
Idioma:
En
Ano de publicação:
1976
Tipo de documento:
Article