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Titolo:
Emerging family of proline-specific peptidases of Porphyromonas gingivalis: Purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV
Autore:
Banbula, A; Bugno, M; Goldstein, J; Yen, J; Nelson, D; Travis, J; Potempa, J;
Indirizzi:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Biochem & Mol Biol, Athens, GA 30602 USA Jagiellonian Univ, Inst Mol Biol, PL-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 l Biol, PL-31120 Krakow, Poland
Titolo Testata:
INFECTION AND IMMUNITY
fascicolo: 3, volume: 68, anno: 2000,
pagine: 1176 - 1182
SICI:
0019-9567(200003)68:3<1176:EFOPPO>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYACRYLAMIDE-GEL ELECTROPHORESIS; BACTEROIDES-GINGIVALIS; CYSTEINE PROTEINASES; COLLAGENOLYTIC ACTIVITY; GLYCYLPROLYL PROTEASE; GENE; PERIODONTITIS; GINGIPAIN; SEQUENCE; INACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Potempa, J Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 ol Biol, Athens, GA 30602 USA
Citazione:
A. Banbula et al., "Emerging family of proline-specific peptidases of Porphyromonas gingivalis: Purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV", INFEC IMMUN, 68(3), 2000, pp. 1176-1182

Abstract

Porphyromonas gingivalis is an asaccharolytic and anaerobic bacterium thatpossesses a complex proteolytic system which is essential for its growth and evasion of host defense mechanisms. In this report, we show the purification and characterization of prolyl dipeptidyl peptidase IV (DPPIV) produced by this organism. The enzyme was purified to homogeneity, and its enzymatic activity and biochemical properties were investigated. P. gingivalis DPPIV, like its human counterpart, is able to cleave the N terminus of synthetic oligopeptides with sequences analogous to those of interleukins 1 beta and 2. Additionally, this protease hydrolyzes biologically active peptides including substance P, fibrin inhibitory peptide, and beta-casomorphin. Southern blot analysis of genomic DNA isolated from several P. gingivalis strains reveal that a single copy of the DPPIV gene was present in all strains tested.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 02:29:11