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Titolo:
INACTIVATION OF ALPHA(1)-PROTEINASE INHIBITOR AS A BROAD SCREEN FOR DETECTING PROTEOLYTIC ACTIVITIES IN UNKNOWN SAMPLES
Autore:
NELSON D; POTEMPA J; TRAVIS J;
Indirizzi:
UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL ATHENS GA 30602 UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL ATHENS GA 30602 JAGIELLONIAN UNIV,DEPT MICROBIOL & IMMUNOL KRAKOW POLAND
Titolo Testata:
Analytical biochemistry (Print)
fascicolo: 2, volume: 260, anno: 1998,
pagine: 230 - 236
SICI:
0003-2697(1998)260:2<230:IOAIAA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA ALPHA-1-PROTEINASE INHIBITOR; PORPHYROMONAS-GINGIVALIS; STAPHYLOCOCCUS-AUREUS; ANTITHROMBIN-III; CYSTIC-FIBROSIS; IV COLLAGENASE; PROTEINASES; PROTEASE; ALPHA-1-ANTICHYMOTRYPSIN; SERPIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
D. Nelson et al., "INACTIVATION OF ALPHA(1)-PROTEINASE INHIBITOR AS A BROAD SCREEN FOR DETECTING PROTEOLYTIC ACTIVITIES IN UNKNOWN SAMPLES", Analytical biochemistry (Print), 260(2), 1998, pp. 230-236

Abstract

The need for a quick, simple screening method for the detection of general proteolytic activity prompted us to determine whether cleavage within the reactive site loop region (RSL) of alpha(1)-proteinase inhibitor (alpha(1)-PI), a well-characterized member of the serpin family known to be susceptible to proteolytic inactivation, can be utilized for this purpose. Inactivation of alpha(1)-PI in the RSL region can be measured by loss of residual inhibitory capacity of alpha(1)-PI againstits target proteinase. While we originally utilized this assay to detect a new proteinase from culture supernatants of Porphyromonas gingivalis, the feasibility of extending this assay to scan for proteolytic activity from other systems was also assessed. As an example, we foundthat the serine proteinase from Staphylococcus aureus (SSP) had virtually the same catalytic efficiency in inactivating alpha(1)-PI in our assay as it did in the hydrolysis of the synthetic substrate Z-Phe-Leu-Glu-pNA (k(cat)/K-m value of 2 x 10(4) M-1 s(-1) vs 2.6 x 10(4) M-1 s(-1), respectively). Additionally, in both assays activity could be readily detected in less than a 1 h incubation at SSP concentrations in the picomolar range. This assay is unique in that proteinases which hydrolyze peptide bonds within the RSL of alpha(1)-PI can readily be detected as measured by loss of alpha(1)-PI inhibitory activity. (C) 1998Academic Press.

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Documento generato il 24/10/20 alle ore 12:06:08