Role of carbohydrate moieties in peanut (Arachis hypogaea) peroxidases.
Biochem J
; 263(1): 129-35, 1989 Oct 01.
Article
em En
| MEDLINE
| ID: mdl-2604691
ABSTRACT
The activities of a cationic (C.PRX) and an anionic peroxidase isolated from peanut (Arachis hypogaea)-cell suspension culture were drastically reduced when they were deglycosylated with glycopeptidase F or oxidized by 10 mM-periodate. In contrast with the controls, the deglycosylated or the oxidized peroxidases were much more susceptible to proteolytic degradation. In radiolabelling experiments with [35S]methionine, the non-glycosylated C.PRX was synthesized in the tunicamycin-treated cultures and secreted into the medium. Examination of the C.PRX polypeptides by SDS/polyacrylamide-gel electrophoresis followed by fluorography showed that the non-glycosylated form had an Mr of approx. 31,000, which is about 78% of that of the glycosylated form. Our results suggest that carbohydrates may not be essential for peroxidase secretion, but that stabilization of the peroxidase molecules and acquisition by these isoenzymes of a catalytically active conformation is linked directly or indirectly to glycosylation.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Arachis
/
Peroxidases
/
Metabolismo dos Carboidratos
/
Isoenzimas
Idioma:
En
Revista:
Biochem J
Ano de publicação:
1989
Tipo de documento:
Article
País de afiliação:
Canadá