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Greber, U F; Kozulic, B; Mosbach, K (1989). Purification of endo-N-acetyl-beta-D-glucosaminidase H by substrate-affinity chromatography. Carbohydrate Research, 189:289-299.

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Abstract

Endo-N-acetyl-beta-D-glucosaminidase H (Endo H) was purified to homogeneity (3000-fold) from a culture filtrate to Streptomyces plicatus. The key step was substrate-affinity chromatography, which afforded a 1000-fold purification and yielded a protease- and exoglycosidase-free preparation of Endo H. Proteins from the crude sample were applied to the substrate-affinity column, consisting of yeast-invertase glycopeptides bound to Sepharose-immobilized concanavalin A. After washing off the unbound proteins, Endo H was quantitatively eluted by methyl alpha-D-mannopyranoside. Various conditions were tested to achieve an optimal binding of Endo H to this substrate-affinity gel. After substrate-affinity chromatography, Endo H was separated from the coeluted gylcopeptide substrate and some protein impurities by gel filtration and hydrophobic chromatography.

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1 citation in Web of Science®
2 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Institute of Molecular Life Sciences
DDC:570 Life sciences; biology
Language:English
Date:15 June 1989
Deposited On:11 Feb 2008 12:16
Last Modified:27 Nov 2013 21:46
Publisher:Elsevier
ISSN:0008-6215
Publisher DOI:10.1016/0008-6215(89)84105-9
PubMed ID:2505925

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