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Characterization of protein glycoforms with N-linked neutral and phosphorylated oligosaccharides: studies on the glycosylation of endoglucanase 1 (Cel7B) from Trichoderma reesei
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
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2001 (English)In: BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, ISSN 0885-4513, Vol. 33, 141-152 p.Article in journal (Refereed) Published
Abstract [en]

Using anion-exchange chromatography the catalytic domain of endoglucanase I (Ce17B) from Trichoderma reesei was resolved in multiple fractions with different isoelectric points, presumably related to different glycoforms of the enzyme. The protein fractio

Place, publisher, year, edition, pages
PORTLAND PRESS , 2001. Vol. 33, 141-152 p.
Keyword [en]
cellulase; fungi; protein glycosylation; CELLOBIOHYDROLASE-I; STRUCTURAL CHARACTERIZATION; CELLULASE; SEQUENCE; QM-9414; GENE; IDENTIFICATION; RESOLUTION; SECRETION; CLEAVAGE
Identifiers
URN: urn:nbn:se:uu:diva-38254OAI: oai:DiVA.org:uu-38254DiVA: diva2:66153
Note
Addresses: Stahlberg J, Univ Uppsala, Ctr Biomed, Dept Mol Biol, POB 590, SE-75124 Uppsala, Sweden. Univ Uppsala, Ctr Biomed, Dept Mol Biol, SE-75124 Uppsala, Sweden. Glycolab, Dept Carbohydrates, Ctr Genet Engn & Biotechnol, Havana, Cuba. Pharmacia & UpjAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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