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Titolo:
Overexpression, purification, and refolding of a Porphyromonas gingivalis cysteine protease from Escherichia coli
Autore:
Margetts, MB; Barr, IG; Webb, EA;
Indirizzi:
CSL Ltd, Div Res & Dev, Parkville, Vic 3052, Australia CSL Ltd Parkville Vic Australia 3052 Dev, Parkville, Vic 3052, Australia
Titolo Testata:
PROTEIN EXPRESSION AND PURIFICATION
fascicolo: 3, volume: 18, anno: 2000,
pagine: 262 - 268
SICI:
1046-5928(200004)18:3<262:OPAROA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-CLONING; PROTEINASE; GINGIPAIN; GENE; W50; PORPHYPAIN; ADHESINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Margetts, MB CSL Ltd, Div Res & Dev, 45 Poplar Rd, Parkville, Vic 3052, Australia CSL Ltd 45 Poplar Rd Parkville Vic Australia 3052 , Australia
Citazione:
M.B. Margetts et al., "Overexpression, purification, and refolding of a Porphyromonas gingivalis cysteine protease from Escherichia coli", PROT EX PUR, 18(3), 2000, pp. 262-268

Abstract

This paper describes the overexpression of the Rgp-1 (arginine) protease domain from Porphyromonas gingivalis. This protease and the related Kgp (lysine) protease, both of which display trypsin-like specificity, have been implicated as major virulence factors and may play a significant role in the etiology of periodontal disease. Both Rgp-1 and Kgp are initially translated as polyproteins, each containing a protease domain and multiple adhesin domains. The Rgp-1 protease domain was expressed in E. coli, purified, refolded, and assayed for activity. These expression studies demonstrated that prior to the formation of inclusion bodies in the E. coli cytoplasm, the protease was proteolytically active and could hydrolyze a specific synthetic substrate. When the Rgp-1 protease domain was purified from inclusion bodiesand refolded, it was found to be autolytically active and displayed specific catalytic activity. This is the first report on the expression and purification of active Rgp-1 from E. coli. Polyclonal antisera raised against recombinant protein recognized the native form of the protease in the P. gingivalis strain W50, indicating that the recombinant protein contained some of the antigenic determinants of the native protease. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 23:42:22