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Titolo:
EXTRACELLULAR NEURAMINIDASE PRODUCTION BY A PASTEURELLA-MULTOCIDA A-3STRAIN ASSOCIATED WITH BOVINE PNEUMONIA
Autore:
WHITE DJ; JOLLEY WL; PURDY CW; STRAUS DC;
Indirizzi:
TEXAS TECH UNIV,HLTH SCI CTR,DEPT MICROBIOL & IMMUNOL LUBBOCK TX 79430 TEXAS TECH UNIV,HLTH SCI CTR,DEPT MICROBIOL & IMMUNOL LUBBOCK TX 79430 USDA ARS,CONSERVAT & PROD RES LAB BUSHLAND TX 79012
Titolo Testata:
Infection and immunity
fascicolo: 5, volume: 63, anno: 1995,
pagine: 1703 - 1709
SICI:
0019-9567(1995)63:5<1703:ENPBAP>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIPOPOLYSACCHARIDES; HAEMOLYTICA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
D.J. White et al., "EXTRACELLULAR NEURAMINIDASE PRODUCTION BY A PASTEURELLA-MULTOCIDA A-3STRAIN ASSOCIATED WITH BOVINE PNEUMONIA", Infection and immunity, 63(5), 1995, pp. 1703-1709

Abstract

The properties of an extracellular neuraminidase produced by a Pasteurella multocida A:3 strain that was isolated in a case of bovine pneumonia were examined during growth in a defined medium. This enzyme (isolated from concentrated culture supernatants of P. multocida, A:3) wasactive against N-acetylneuramin lactose, human alpha-1-acid glycoprotein, fetuin, colominic acid, and bovine submaxillary mucin. Enzyme elaboration was correlated with the growth of the organism in a defined medium, with maximum quantities produced in the stationary phase. The enzyme was purified by a combination of ammonium sulfate fractionation,ion exchange on DEAE Sephacel, and gel filtration on Sephadex G-200. The purified neuraminidase possessed a specific activity of 9.36 mu mol of sialic acid released per min per mg of protein against fetuin. The enzyme possessed a pH optimum of 6.0 and a K-m of 0.03 mg/ml. The P.multocida A:3 neuraminidase had a molecular weight of approximately 500,000 as estimated by gel filtration. The enzyme was stable at 4 and 37 degrees C for 3 h. Approximately 75% of the neuraminidase activity was lost within 30 min at 50 degrees C. Greater than 90% of the enzymeactivity was destroyed within 10 min at temperatures of greater than or equal to 65 degrees C. The P. multocida neuraminidase does not appear to be serologically related to the Pasteurella haemolytica A1 neuraminidase since antiserum prepared against the purified P. haemolytica enzyme did not neutralize the P. multocida enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/10/20 alle ore 14:47:22