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Titolo:
Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis
Autore:
Dubin, G; Chmiel, D; Mak, P; Rakwalska, M; Rzychon, M; Dubin, A;
Indirizzi:
Jagiellonian Univ, Inst Mol Biol, PL-30387 Krakow, Poland Jagiellonian Univ Krakow Poland PL-30387 l Biol, PL-30387 Krakow, Poland
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 11, volume: 382, anno: 2001,
pagine: 1575 - 1582
SICI:
1431-6730(200111)382:11<1575:MCABCO>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
SODIUM DODECYL-SULFATE; AUREUS; SEQUENCE; GENE; AGR; PURIFICATION; PROTEINASE; ELASTASE; SITE;
Keywords:
protease; proteinase; staphopain; Staphylococcus epidermidis; staphylopain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Dubin, A Jagiellonian Univ, Inst Mol Biol, 7 Gronostajowa Str, PL-30387 Krakow, Poland Jagiellonian Univ 7 Gronostajowa Str Krakow Poland PL-30387 land
Citazione:
G. Dubin et al., "Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis", BIOL CHEM, 382(11), 2001, pp. 1575-1582

Abstract

We report the complete coding sequence and the partial amino acid sequence(determined by chemical sequencing) of Staphylococcus epidermidis extracellular cysteine (Ecp) and serine (Esp) proteases. The first enzyme shows an extended sequence similarity to Staphylococcus aureus cysteine protease (staphopain) and the second one resembles the serine protease produced by thatspecies. The region directly upstream of the sequence coding for the mature protein in both enzymes displays significant homology to the profragmentsencoded by sspB and sspA, respectively, thus suggesting that the characterised enzymes may also be produced as proproteins. Furthermore, we report some biological properties of the cysteine protease, contributing to a betterunderstanding of its role as a possible virulence factor. The proteolytic activity of this enzyme was rapidly and efficiently inhibited by human alpha -2-macroglobulin; however, human kininogen as well as cystatins (A, C andD) were not inhibitory. Moreover, the protease was capable of inactivating, by limited proteolysis, both a-l-antitrypsin and HMW-kininogen, but neither alpha -1-antichymotrypsin nor antithrombin Ill.

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Documento generato il 04/12/20 alle ore 22:29:18