Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
AN INVESTIGATION INTO THE USE OF SDS-PAGE OF CELL-SURFACE EXTRACTS AND PROTEOLYTIC ACTIVITY TO DIFFERENTIATE PREVOTELLA-NIGRESCENS AND PREVOTELLA-INTERMEDIA
Autore:
COOKSON AL; WRAY A; HANDLEY PS; JACOB AE;
Indirizzi:
UNIV MANCHESTER,SCH BIOL SCI,2205 STOPFORD BLDG,OXFORD RD MANCHESTER M13 9PT LANCS ENGLAND UNIV MANCHESTER,SCH BIOL SCI MANCHESTER M13 9PT LANCS ENGLAND
Titolo Testata:
FEMS microbiology letters
fascicolo: 2, volume: 136, anno: 1996,
pagine: 109 - 115
SICI:
0378-1097(1996)136:2<109:AIITUO>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS W50; SP-NOV; PROPOSAL;
Keywords:
PREVOTELLA INTERMEDIA; PREVOTELLA NIGRESCENS; SDS-PAGE; PROTEASES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
13
Recensione:
Indirizzi per estratti:
Citazione:
A.L. Cookson et al., "AN INVESTIGATION INTO THE USE OF SDS-PAGE OF CELL-SURFACE EXTRACTS AND PROTEOLYTIC ACTIVITY TO DIFFERENTIATE PREVOTELLA-NIGRESCENS AND PREVOTELLA-INTERMEDIA", FEMS microbiology letters, 136(2), 1996, pp. 109-115

Abstract

By comparison of the cell surface proteins derived from the outer membrane and fibrils from 14 Prevotella intermedin and 19 Prevotella nigrescens strains using SDS and analysed by SDS-PAGE, it was possible to distinguish the two species. A polypeptide of approx. 21 kDa distinguished P. intermedia strains, whereas two polypeptides of approx. 18 and22 kDa could be used to identify P, nigrescens strains. Four other human oral black pigmented bacterial species (Porphyromonas gingivalis, Prevotella denticola, Prevotella loescheii and Prevotella melaninogenica) did not have the 18-, 21- or 22-kDa polypeptides shown by P. intermedia or P, nigrescens. The cell-associated proteolytic activity of eight strains of P. intermedia, 14 strains of P. nigrescens and one strain of P. gingivalis (W50) was assessed using four chromogenic substrates. The hydrolysis of the substrate GPPNA (indicative of dipeptidyl peptidase IV-like activity) and SAAAPNA (elastase-like activity) by P. intermedia strains varied from 32 to 114 units and 0.5 to 12.6 units ofactivity respectively, where one unit was defined as the amount of protease enzyme catalysing the formation of I nmol of p-nitroaniline under experimental conditions. 37.5% (3 of 8) of P. intermedia strains hydrolysed SAAPPPNA (chymotrypsin-like enzyme activity) with activities of between 7 and 12 units. The hydrolysis;of GPPNA and SAAAPNA by P. nigrescens strains was 32-149 and 3-16 units, respectively. 57% (8 of 14) of P. nigrescens strains hydrolysed SAAPPPNA with activities ranging from 3 to 8 units. None of the P. intermedia or P. nigrescens strains examined were found to have trypsin-like enzyme activity (BAPNA hydrolysis). The GPPNA and SAAAPNA hydrolytic activity associated with theproteases from Porphyromonas gingivalis W50 was at least twice that of P. intermedia and P. nigrescens strains, The similar peptidase activities of P. intermedia and P. nigrescens against chromogenic substrates cannot be used to differentiate the species, but SDS-PAGE of cell surface protein extracts allowed unambiguous speciation between P. intermedia and P. nigrescens. This simple technique of cell surface proteinanalysis can be performed in most laboratories and offers a convenient way by which to differentiate the two species.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:28:02