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Titolo:
DIFFERENTIATION OF THERMOLYSINS AND SERRALYSINS BY MONOCLONAL-ANTIBODIES
Autore:
KOOI C; SOKOL PA;
Indirizzi:
UNIV CALGARY,HLTH SCI CTR,DEPT MICROBIOL & INFECT DIS CALGARY AB T2N 4N1 CANADA UNIV CALGARY,HLTH SCI CTR,DEPT MICROBIOL & INFECT DIS CALGARY AB T2N 4N1 CANADA
Titolo Testata:
Journal of Medical Microbiology
fascicolo: 3, volume: 45, anno: 1996,
pagine: 219 - 225
SICI:
0022-2615(1996)45:3<219:DOTASB>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PNEUMOPHILA ZINC METALLOPROTEASE; PSEUDOMONAS-AERUGINOSA ELASTASE; LEGIONELLA-PNEUMOPHILA; NUCLEOTIDE-SEQUENCE; MOLECULAR CHARACTERIZATION; HEMAGGLUTININ PROTEASE; STRUCTURAL GENE; PROTEINS; LASA; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
C. Kooi e P.A. Sokol, "DIFFERENTIATION OF THERMOLYSINS AND SERRALYSINS BY MONOCLONAL-ANTIBODIES", Journal of Medical Microbiology, 45(3), 1996, pp. 219-225

Abstract

Two monoclonal antibodies (MAbs) to a 36-kDa extracellular metalloprotease (PSCP) from Burkholderia (Pseudomonas) cepacia were found to react with thermolysin, Pseudomonas aeruginosa elastase, alkaline protease (Apr) and LasA, Serratia marcescens protease (SMP), Aeromonas hydrophila protease (AhP), and both the lethal factor (LF) and protective antigen (PA) of Bacillus anthracis on immunoblots. The MAbs were capableof neutralising the proteolytic activity of thermolysin, P. aeruginosa elastase and PSCP but trot that of Apr, SMP, and AhP. These results suggest that these MAbs may be able to differentiate between the thermolysin and serralysin family of metalloproteases on the basis of theirneutralisation capability and could, therefore, be useful tools in the characterisation of new bacterial proteases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 13:42:56