Heterogeneous glycosylation of cationic peanut peroxidase
| Autor: | Mark Gijzen, Robert B. van Huystee, Lianglu Wan |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Glycosylation
Arachis Biochemistry Suspension culture Chromatography Affinity chemistry.chemical_compound Polysaccharides Concanavalin A Molecular Biology Cells Cultured Chromatography High Pressure Liquid biology Cationic polymerization Cell Biology Complex type beta-Galactosidase Isoenzymes Peroxidases chemistry Galactose Chromatography Gel biology.protein Electrophoresis Polyacrylamide Gel Asparagine Isoelectric Focusing Plant Lectins Protein Binding Peroxidase |
| Zdroj: | Biochemistry and Cell Biology. 72:411-417 |
| ISSN: | 1208-6002 0829-8211 |
| DOI: | 10.1139/o94-055 |
| Popis: | Cationic peanut peroxidase (CPrx) from a cell suspension culture is N-glycosylated at Asn60, Asn144, and Asn185. All three N-glycans are complex type and galactose rich, and show heterogeneity in length and ConA (concanavalin A) binding property. The glycan heterogeneity causes a polymorphism of the enzyme. Based on its behavior on ConA columns, CPrx can be grouped into two fractions: nonbinding (CPrx−) and binding (CPrx+) types. A synchronously cosecreted β-galactosidase has been discovered in the culture medium; there are two isozymes of 60 kDa (pI 7.3) and 66 kDa (pI 7.6). This β-galactosidase has been partially purified by a combination of ion-exchange and size-exclusion chromatographies and preparative isoelectrofocusing. In vitro experiments indicate that the cosecreted β-galactosidase is able to convert peroxidase from CPrx− to CPrx+ and may, to some extent, contribute to the glycan heterogeneity of peroxidase in the cell culture.Key words: peroxidase, peanut, glycan, heterogeneity, β-galactosidase. |
| Databáze: | OpenAIRE |
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