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Titolo:
Avidin is a promising tag for fusion proteins produced in baculovirus-infected insect cells
Autore:
Airenne, KJ; Laitinen, OH; Alenius, H; Mikkola, J; Kalkkinen, N; Arif, SAM; Yeang, HY; Palosuo, T; Kulomaa, MS;
Indirizzi:
Univ Jyvaskyla, Dept Biol & Environm Sci, FIN-40100 Jyvaskyla, Finland Univ Jyvaskyla Jyvaskyla Finland FIN-40100 FIN-40100 Jyvaskyla, Finland Finnish Inst Occupat Hlth, Helsinki, Finland Finnish Inst Occupat Hlth Helsinki Finland upat Hlth, Helsinki, Finland Natl Publ Hlth Inst, Helsinki, Finland Natl Publ Hlth Inst Helsinki Finland Publ Hlth Inst, Helsinki, Finland Univ Helsinki, Inst Biotechnol, Helsinki, Finland Univ Helsinki HelsinkiFinland inki, Inst Biotechnol, Helsinki, Finland Rubber Res Inst, Kuala Lumpur, Malaysia Rubber Res Inst Kuala Lumpur Malaysia Res Inst, Kuala Lumpur, Malaysia
Titolo Testata:
PROTEIN EXPRESSION AND PURIFICATION
fascicolo: 1, volume: 17, anno: 1999,
pagine: 139 - 145
SICI:
1046-5928(199910)17:1<139:AIAPTF>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
TREE HEVEA-BRASILIENSIS; RECOMBINANT PROTEINS; ESCHERICHIA-COLI; PURIFICATION; STREPTAVIDIN; IMMOBILIZATION; DERIVATIVES; GENERATION; LATEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Kulomaa, MS Univ Jyvaskyla, Dept Biol & Environm Sci, POB 35, FIN-40351 Jyvaskyla, Finland Univ Jyvaskyla POB 35 Jyvaskyla Finland FIN-40351 la, Finland
Citazione:
K.J. Airenne et al., "Avidin is a promising tag for fusion proteins produced in baculovirus-infected insect cells", PROT EX PUR, 17(1), 1999, pp. 139-145

Abstract

The baculovirus expression vector system (BEVS) has become one of the mostversatile and powerful eukaryotic systems for recombinant protein expression. We have constructed a novel baculovirus transfer vector (pbacAVs+C) which allows for the efficient production, detection, and single-step purification of the desired molecule as a secretion-compatible avidin fusion protein in insect cells. It also enables fast construction of the baculoviruses by site-specific transposition in Escherichia coli. To demonstrate the powerof this vector, we report here on the production of immunologically intacthevein, a major cysteine-rich latex allergen, as avidin fusion protein. Our results indicate that avidin is a stable and versatile tag in the BEVS. It retains its extraordinarily high biotin-binding activity and also enablesindependent folding of the fusion partner. The versatility with which avidin fusion proteins can be detected, purified, and immobilized is the basis for the use of our system as a useful alternative in eukaryotic fusion protein production. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 03:50:23