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Titolo:
Purification and characterization of hemolysin from Porphyromonas gingivalis A7436
Autore:
Deshpande, RG; Khan, MB;
Indirizzi:
Morehouse Sch Med, Dept Microbiol & Immunol, Atlanta, GA 30310 USA Morehouse Sch Med Atlanta GA USA 30310 l & Immunol, Atlanta, GA 30310 USA
Titolo Testata:
FEMS MICROBIOLOGY LETTERS
fascicolo: 2, volume: 176, anno: 1999,
pagine: 387 - 394
SICI:
0378-1097(19990715)176:2<387:PACOHF>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS; CYSTEINE PROTEINASE; ESCHERICHIA-COLI; VIRULENCE; GENE; CLONING; HEMIN; W50;
Keywords:
hemolysin; Ni-NTA chromatography; Porphyromonas gingivalis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Deshpande, RG Morehouse Sch Med, Dept Microbiol & Immunol, 720 Westview Dr, Atlanta, GA 30310 USA Morehouse Sch Med 720 Westview Dr Atlanta GA USA 30310 0 USA
Citazione:
R.G. Deshpande e M.B. Khan, "Purification and characterization of hemolysin from Porphyromonas gingivalis A7436", FEMS MICROB, 176(2), 1999, pp. 387-394

Abstract

Porphyromonas gingivalis, a periodontal pathogen, has the ability to lyse erythrocytes. The hemolytic activity of P. gingivalis A7436 was purified asa 45-kDa protein from the culture supernatant of a 3-days old culture using nickel-nitrilotriacetic acid chromatography. Erythrocytes treated with purified P. gingivalis hemolysin showed the presence of pores and extracellular debris by scanning electron microscopy. Active immunization of mice with15 mu g hemolysin induced neutralizing antibodies to hemolysin. Heating at60 degrees C and treatment with trypsin and dithiothreitol abolished hemolytic activity, while incubation with the protease inhibitor Na-p-tosyl-L-lysine chloromethyl ketone caused no effect. We report here for the first time purification of a hemolysin from P. gingivalis A7436. The amino acid sequence of an internal peptide of hemolysin showed sequence similarity with fimbrillin from P. gingivalis HG564. However, the amino acid composition of purified hemolysin was different from that of P. gingivalis fimbrillin. Also, the ability to lyse but not agglutinate erythrocytes and to bind to nickel-nitrilotriacetic acid differentiates P. gingivalis hemolysin from fimbrillin. (C) 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 19:05:55