Author | Lopes, Andréa | |
Author | Coelho, Rosalie R. R. | |
Author | Meirelles, Maria Nazareth L. | |
Author | Branquinha, Marta Helena | |
Author | Vermelho, Alane Beatriz | |
Access date | 2020-10-17T18:52:00Z | |
Available date | 2020-10-17T18:52:00Z | |
Document date | 1999 | |
Citation | LOPES, Andréa et al. Extracellular Serine-proteinases Isolated from Streptomyces alboniger: Partial Characterization and Effect of Aprotinin on Cellular Structure. Memórias do Instituto Oswaldo Cruz, Rio de Janeiro, v. 94, n. 6, p. 763-779, Nov./Dec. 1999. | pt_BR |
ISSN | 0074-0276 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/44031 | |
Language | eng | pt_BR |
Publisher | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. | pt_BR |
Rights | open access | pt_BR |
Subject in Portuguese | Streptomyces alboniger | pt_BR |
Subject in Portuguese | Aprotinina | pt_BR |
Subject in Portuguese | Crescimento | pt_BR |
Subject in Portuguese | Serine-proteinases | pt_BR |
Title | Extracellular Serine-proteinases Isolated from Streptomyces alboniger: Partial Characterization and Effect of Aprotinin on Cellular Structure | pt_BR |
Type | Article | pt_BR |
DOI | 10.1590/S0074-02761999000600010 | |
Abstract | 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% and 10.4% yield, respectively. The optimum pH for the proteinases activity, using
α-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 µg/ml, 10 µg/ml of aprotinin was used, being completely inhibited with 20 µg/ml and
40 µg/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. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Professor Paulo de Góes. Departamento de Microbiologia Geral. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Professor Paulo de Góes. Departamento de Microbiologia Geral. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Ultra-estrutura e Biologia Celular. Laboratório de Ultraestrutura Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Professor Paulo de Góes. Departamento de Microbiologia Geral. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Microbiologia Professor Paulo de Góes. Departamento de Microbiologia Geral. Rio de Janeiro, RJ, Brasil. | pt_BR |
Subject | Streptomyces alboniger | pt_BR |
Subject | Serine-proteinases | pt_BR |
Subject | Growth | pt_BR |
Subject | Aprotinin | pt_BR |
e-ISSN | 1678-8060 | |