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Titolo:
Specific glycosidase activity isolated from a random phage display antibody library
Autore:
Goud, GN; Artsaenko, O; Bols, M; Sierks, M;
Indirizzi:
Univ Maryland Baltimore Cty, Dept Chem & Biochem Engn, Baltimore, MD 21250USA Univ Maryland Baltimore Cty Baltimore MD USA 21250 Baltimore, MD 21250USA Aarhus Univ, Dept Chem, DK-8000 Aarhus C, Denmark Aarhus Univ Aarhus Denmark C Univ, Dept Chem, DK-8000 Aarhus C, Denmark
Titolo Testata:
BIOTECHNOLOGY PROGRESS
fascicolo: 1, volume: 17, anno: 2001,
pagine: 197 - 202
SICI:
8756-7938(200101/02)17:1<197:SGAIFA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSITION-STATE ANALOG; CARBOHYDRATE INTERACTIONS; MELANOMA-CELLS; AFFINITY; RECOGNITION; SELECTION; BINDING; LECTIN; OLIGOSACCHARIDES; IMMUNIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Sierks, M Univ Maryland Baltimore Cty, Dept Chem & Biochem Engn, 1000 Hilltop Circle, Baltimore, MD 21250 USA Univ Maryland Baltimore Cty 1000 Hilltop Circle Baltimore MD USA 21250
Citazione:
G.N. Goud et al., "Specific glycosidase activity isolated from a random phage display antibody library", BIOTECH PR, 17(1), 2001, pp. 197-202

Abstract

Carbohydrates serve as key receptor sites in various cellular events such as viral attachment, tumor formation, and tissue inflammation. A potential route to control these events is to manipulate targeted carbohydrate structures in vivo using specifically designed glycohydrolases. Here we show thata stereospecific catalytic activity designed toward a particular sugar andlinkage can be readily isolated from a phage display antibody library derived from a nonimmunized host. The activity was isolated using a transition-state analogue mimicking an alpha -glucosidasic linkage as antigen and showed a 20-fold specificity for that sugar and linkage. The DNA sequence, however, contains a large deletion in the antibody gene, which also changes thedownstream reading frame, resulting in a translated sequence containing only 57 amino acids that has a predominantly hydrophobic amino terminal and astrongly hydrophilic carboxy terminal. The isolated catalytic activity hasa strong pH dependence, attributable to one or more of the numerous potentially charged groups in the carboxyl terminal. While the protein readily forms more stable multimers, the 7.3-kD monomer represents by far the smallest glycosidase enzyme reported to date and can provide substantial new information toward understanding and modifying glycosidase activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 01:03:15