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Titolo:
Identification and properties of two extracellular proteases from Brevundimonas diminuta
Autore:
Chaia, AA; Giovanni-De-Simone, S; Petinate, SDG; Lima, APCD; Branquinha, MH; Vermelho, AB;
Indirizzi:
Univ Fed Rio de Janeiro, CCS, Inst Microbiol Prof Paulo de Goes, Dept Microbiol Geral, BR-21949900 Rio De Janeiro, Brazil Univ Fed Rio de Janeiro Rio De Janeiro Brazil BR-21949900 BCeiro, Brazil FIOCRUZ, Dept Bioquim & Biol Mol, BR-21045900 Rio De Janeiro, Brazil FIOCRUZ Rio De Janeiro Brazil BR-21045900 BC45900 Rio De Janeiro, Brazil Univ Fed Fluminense, Inst Biol, Dept Biol Celular & Mol, Rio De Janeiro, Brazil Univ Fed Fluminense Rio De Janeiro Brazil & Mol, Rio De Janeiro, Brazil Univ Fed Rio de Janeiro, Inst Biofis Carlos Chagas Filho, BR-21941 Rio De Janeiro, Brazil Univ Fed Rio de Janeiro Rio De Janeiro Brazil BR-21941 e Janeiro, Brazil
Titolo Testata:
BRAZILIAN JOURNAL OF MICROBIOLOGY
fascicolo: 1, volume: 31, anno: 2000,
pagine: 25 - 29
SICI:
1517-8382(200001/03)31:1<25:IAPOTE>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSEUDOMONAS-DIMINUTA; PURIFICATION; PHOSPHOTRIESTERASE;
Keywords:
metalloproteases; Brevundimonas diminuta; Pseudomonadaceae; extracellular proteases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Chaia, AA Univ Fed Rio de Janeiro, CCS, Inst Microbiol Prof Paulo de Goes,Dept Microbiol Geral, Bl I, BR-21949900 Rio De Janeiro, Brazil Univ Fed Rio de Janeiro Bl I Rio De Janeiro Brazil BR-21949900 BC
Citazione:
A.A. Chaia et al., "Identification and properties of two extracellular proteases from Brevundimonas diminuta", BRAZ J MICR, 31(1), 2000, pp. 25-29

Abstract

Extracellular proteases from Brevundimonas diminuta (syn. Pseudomonas diminuta) were studied in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) containing a copolymerized substrate. Two proteases were detected migrating at 67 kDa and 50 kDa: both of them hydrolysed preferentially gelatin, but casein was also degraded and a slight hydrolysis was observed with hemoglobin; No detectable extracellular proteolytic activity was found in bovine serum albumin-containing gels. The optima temperature and pH for proteolytic activity were between 40 degreesC and 50 degreesC in a pH ranging from 7.0 to 11.0, respectively These enzymes were isolated by analytical high performance liquid chromatography (HPLC). Protease assays with the synthetic substrate Z-Phe-Arg-MCA and the inhibitors EGTA, EDTA and 1, 10phenanthroline point out that these enzymes are metalloproteases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/11/20 alle ore 21:36:08