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Titolo:
A family 2a carbohydrate-binding module suitable as an affinity tag for proteins produced in Pichia pastoris
Autore:
Boraston, AB; McLean, BW; Guarna, MM; Amandaron-Akow, E; Kilburn, DG;
Indirizzi:
Univ British Columbia, Biotechnol Lab, Vancouver, BC V6T 1Z3, Canada Univ British Columbia Vancouver BC Canada V6T 1Z3 ver, BC V6T 1Z3, Canada Univ British Columbia, Prot Engn Network Ctre Excellence, Vancouver, BC V6T 1Z3, Canada Univ British Columbia Vancouver BC Canada V6T 1Z3 ver, BC V6T 1Z3, Canada Univ British Columbia, Dept Microbiol & Immunol, Vancouver, BC V6T 1Z3, Canada Univ British Columbia Vancouver BC Canada V6T 1Z3 ver, BC V6T 1Z3, Canada
Titolo Testata:
PROTEIN EXPRESSION AND PURIFICATION
fascicolo: 3, volume: 21, anno: 2001,
pagine: 417 - 423
SICI:
1046-5928(200104)21:3<417:AF2CMS>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
N-LINKED OLIGOSACCHARIDES; DOMAIN FUSION PROTEIN; CELLULOMONAS-FIMI; ESCHERICHIA-COLI; GLYCOSYLATION; EXPRESSION; EXOGLUCANASE; TRYPTOPHAN; YEAST;
Keywords:
cellulose-binding domain; carbohydrate-binding module; stem-cell factor; glycosylation; Pichia pastoris;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Kilburn, DG Univ British Columbia, Biotechnol Lab, 237,6174 Univ Blvd, Vancouver, BC V6T 1Z3, Canada Univ British Columbia 237,6174 Univ Blvd Vancouver BC Canada V6T 1Z3
Citazione:
A.B. Boraston et al., "A family 2a carbohydrate-binding module suitable as an affinity tag for proteins produced in Pichia pastoris", PROT EX PUR, 21(3), 2001, pp. 417-423

Abstract

The family 2a carbohydrate-binding module (CBM), Ce15ACBM2a, from the C-terminus of Ce15A from Cellulomonas fimi, and Xyn10ACBM2a, the family 2a CBM from the C-terminus of Xyn10A from C. fimi, were compared as fusion partners for proteins produced in the methylotrophic yeast Pichia pastoris. G;ene fusions of murine stem-cell factor (SCF) with both CBMs were expressed in P. pastoris. The secreted SCF-Xyn10ACBM2a polypeptides were highly glycosylated and bound poorly to cellulose. In contrast, fusion of SCF to Ce15ACBM2a, which lacks potential N-linked glycosylation sites, resulted in the production of polypeptides which bound tightly to cellulose. Cloning and expression of these CBM2a in P. pastoris without a fusion partner confirmed that N-linked glycosylation at several sites was responsible for the poor cellulose binding. The nonglycosylated CBMs produced in E. coli had very similar cellulose-binding properties. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 11:01:50