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Titolo:
CLONING AND CHARACTERIZATION OF A NEW PROTEASE GENE (PRTH) FROM PORPHYROMONAS-GINGIVALIS
Autore:
FLETCHER HM; SCHENKEIN HA; MACRINA FL;
Indirizzi:
VIRGINIA COMMONWEALTH UNIV,DEPT MICROBIOL & IMMUNOL RICHMOND VA 23298 VIRGINIA COMMONWEALTH UNIV,CLIN RES CTR PERIODONTAL DIS RICHMOND VA 23298
Titolo Testata:
Infection and immunity
fascicolo: 10, volume: 62, anno: 1994,
pagine: 4279 - 4286
SICI:
0019-9567(1994)62:10<4279:CACOAN>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLACK-PIGMENTED BACTEROIDES; COLLAGENASE ACTIVITY; POLYACRYLAMIDE GELS; MOLECULAR-CLONING; SEQUENCE-ANALYSIS; ESCHERICHIA-COLI; DNA; NITROCELLULOSE; EXPRESSION; PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
H.M. Fletcher et al., "CLONING AND CHARACTERIZATION OF A NEW PROTEASE GENE (PRTH) FROM PORPHYROMONAS-GINGIVALIS", Infection and immunity, 62(10), 1994, pp. 4279-4286

Abstract

Porphyromonas gingivalis has been implicated as a contributing etiological agent of adult periodontitis and generalized forms of early-onset periodontitis. Proteases of P. gingivalis may contribute to its pathogenicity by destroying connective tissue as well as inactivating keg plasma proteins that might mediate protective host functions. In orderto explore this problem, antiserum raised against membrane vesicles of P. gingivalis W83 was used to screen a genomic library of strain W83constructed by using the lambda DASH vector system. A recombinant phage (lambda 34) expressing a P. gingivalis protease from the library was identified and characterized. Casein substrate zymography of lambda 34 lysates revealed a protease with an apparent molecular mass of 97 kDa. The gene encoding this protease was designated prtH. It was localized to a 3.7-kb HindIII-BamHI fragment and specified an enzyme which hydrolyzed the human C3 complement protein under defined conditions. The nucleotide sequence of this 3.7-kb fragment was determined, and one 2.9-kb open reading frame (992 amino acids) corresponding to a 110-kDaprotein was detected, suggesting it might be a precursor of the 97-kDa active protease. prtH is not similar to any previously cloned protease gene from P. gingivalis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 21:57:55