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Titolo:
CHARACTERIZATION OF THE TRYPSIN-LIKE ACTIVITY OF BACTEROIDES-FORSYTHUS
Autore:
GRENIER D;
Indirizzi:
UNIV LAVAL,FAC MED DENT,RECH ECOL BUCCALE GRP ST FOY PQ G1K 7P4 CANADA
Titolo Testata:
Microbiology
, volume: 141, anno: 1995,
parte:, 4
pagine: 921 - 926
SICI:
1350-0872(1995)141:<921:COTTAO>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
DESTRUCTIVE PERIODONTAL-DISEASES; API-ZYM SYSTEM; PURIFICATION; BACTERIA;
Keywords:
BACTEROIDES FORSYTHUS; TRYPSIN-LIKE ACTIVITY; PROTEASE; PERIODONTAL DISEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
D. Grenier, "CHARACTERIZATION OF THE TRYPSIN-LIKE ACTIVITY OF BACTEROIDES-FORSYTHUS", Microbiology, 141, 1995, pp. 921-926

Abstract

Bacteroides forsythus, a bacterial species frequently associated withdiseased periodontal sites, is known to possess trypsin-like activity. The present study was undertaken to determine the major characteristics of this activity. The trypsin-like activity was mainly found on the surface of the bacteria and could be solubilized with a zwitterionicdetergent (Zwittergent 3-14), Using N-alpha-benzoyl-DL-arginine-p-nitroanilide as substrate, the optimum ph was between 7.5 and 8.5 and theoptimum temperature was 35 degrees C. The evidence suggests that the enzyme is a serine protease since it was strongly inhibited by diisopropylfluorophosphate (DFP), N-alpha-p-tosyl-L-lysine chloromethyl ketone hydrochloride, leupeptin and antipain. The B. forsythus trypsin-likeenzyme cleaved numerous chromogenic synthetic peptides containing either an arginine or lysine bond, but could not hydrolyse native proteins including casein, gelatin and BSA. Incubation of a cell envelope extract of B, forsythus in the presence of [H-3]DFP, which is known to bind irreversibly to serine proteases, labelled two bands at 70 and 81 kDa following SDS-PAGE (under reducing conditions) and fluorography. Itis suggested that the B, forsythus trypsin-like enzyme may be mainly involved in the degradation of small peptides resulting from hydrolysis of larger proteins by other oral bacteria.

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Documento generato il 28/11/20 alle ore 21:53:32