Purification of exopolygalacturonase by affinity chromatography on Concanavalin A — Bead cellulose

Autor:	Mária Dzúrová, Danica Mislovičová, Eva Stratilová
Rok vydání:	1996
Předmět:	chemistry.chemical_classification Chromatography biology Applied Microbiology and Biotechnology Biochemistry chemistry.chemical_compound Enzyme chemistry Affinity chromatography Concanavalin A biology.protein Cellulose Glycoprotein Triazine
Zdroj:	Scopus-Elsevier
ISSN:	1573-6784 0951-208X
DOI:	10.1007/bf00173256
Popis:	Interaction of exopolygalacturonase isolated from carrot roots with Concanavalin A was investigated. The glycoprotein character of this enzyme was confirmed. Using affinity chromatography on Concanavalin A — triazine bead cellulose about fifty fold purification was achieved. The individual enzyme forms were not separated by this method, which might imply identical or similar pattern of n-glycosylation.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ed2d3be464ff05fa279af4391e93c35 https://doi.org/10.1007/bf00173256 Zobrazit plný text záznamu Full text from SpringerLink