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Extracellular serine-proteinases isolated from Streptomyces alboniger: Partial characterization and effect of aprotinin on cellular structure
Lopes, Andréa; Coelho, Rosalie R. R; Meirelles, Maria Nazareth L; Branquinha, Marta Helena; Vermelho, Alane Beatriz.
  • Lopes, Andréa; Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Professor Paulo de Góes. Departamento de Microbiologia Geral.
  • Coelho, Rosalie R. R; Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Professor Paulo de Góes. Departamento de Microbiologia Geral.
  • Meirelles, Maria Nazareth L; Instituto Oswaldo Cruz. Departamento de Ultra-estrutura e Biologia Celular. Laboratório de Ultraestrutura Celular.
  • Branquinha, Marta Helena; Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Professor Paulo de Góes. Departamento de Microbiologia Geral.
  • Vermelho, Alane Beatriz; Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Professor Paulo de Góes. Departamento de Microbiologia Geral.
Mem. Inst. Oswaldo Cruz ; 94(6): 763-70, Nov.-Dec. 1999.
Artículo en Inglés | LILACS | ID: lil-251336
RESUMO
Streptomyces alboniger ATCC 12461 grown in brain heart infusion (BHI) medium produced two extracellular serine-proteinases, denoted SP I and SP II, which were purified by ammonium sulfate precipitation and aprotinin-agarose affinity chromatography. SP I was purified 88,9-fold and SP II 66,7- fold, with 33.4 percent and 10.4 percent yield, respectively. The optimum pH for the proteinases activity, using a-N-p-tosyl-L-arginine-methyl ester (TAME) as substrate, was 9-10 and the optimum temperature was 37ºC. The proteolytic activity of SP I and SP II was inhibited by aprotinin and SP I was partially inhibited by leupeptin, both serine-proteinase inhibitors. S. alboniger growth in BHI-liquid medium decreased when 5 mg/ml, 10 mg/ml of aprotinin was used, being completely inhibited with 20 mg/ml and 40 mg/ml. At the ultrastructural level, aprotinin-treated S. alboniger cells showed swelling of the bacterial body and condensation of the genetic material, probably related to the inhibition of its growth
Asunto(s)
Texto completo: Disponible Índice: LILACS (Américas) Asunto principal: Streptomyces / Serina Endopeptidasas / Inhibidores de Serina Proteinasa / Aprotinina Idioma: Inglés Revista: Mem. Inst. Oswaldo Cruz Asunto de la revista: Medicina Tropical / Parasitología Año: 1999 Tipo del documento: Artículo País de afiliación: Brasil

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Texto completo: Disponible Índice: LILACS (Américas) Asunto principal: Streptomyces / Serina Endopeptidasas / Inhibidores de Serina Proteinasa / Aprotinina Idioma: Inglés Revista: Mem. Inst. Oswaldo Cruz Asunto de la revista: Medicina Tropical / Parasitología Año: 1999 Tipo del documento: Artículo País de afiliación: Brasil