Extracellular serine-proteinases isolated from Streptomyces alboniger: Partial characterization and effect of aprotinin on cellular structure
Mem. Inst. Oswaldo Cruz
; 94(6): 763-70, Nov.-Dec. 1999.
Article
en En
| LILACS
| ID: lil-251336
Biblioteca responsable:
BR1.1
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
Texto completo:
1
Colección:
01-internacional
Base de datos:
LILACS
Asunto principal:
Streptomyces
/
Serina Endopeptidasas
/
Inhibidores de Serina Proteinasa
/
Aprotinina
Idioma:
En
Revista:
Mem. Inst. Oswaldo Cruz
Asunto de la revista:
MEDICINA TROPICAL
/
PARASITOLOGIA
Año:
1999
Tipo del documento:
Article
País de afiliación:
Brasil
Pais de publicación:
Brasil