Author | Xavier, Luciana Pereira | |
Author | Oliveira, Maria Goreti Almeida | |
Author | Guedes, Raul Narciso Carvalho | |
Author | Santos, Agenor Valadares | |
Author | De Simone, Salvatore Giovanni | |
Access date | 2019-12-12T16:14:57Z | |
Available date | 2019-12-12T16:14:57Z | |
Document date | 2005 | |
Citation | XAVIER, Luciana Pereira et al. Trypsin-like activity of membrane-bound midgut proteases from Anticarsia gemmatalis (Lepidoptera: Noctuidae). Eur. J. Entomol., v. 102, p. 147-153, 2005. | pt_BR |
ISSN | 1802-8829 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/37912 | |
Language | eng | pt_BR |
Publisher | European Journal of Entomology | pt_BR |
Rights | open access | pt_BR |
Subject in Portuguese | Tripsina | pt_BR |
Subject in Portuguese | Proteases | pt_BR |
Subject in Portuguese | Lepidópteros | pt_BR |
Title | Trypsin-like activity of membrane-bound midgut proteases from Anticarsia gemmatalis (Lepidoptera: Noctuidae) | pt_BR |
Type | Article | pt_BR |
DOI | 10.14411/eje.2005.023 | |
Abstract | Membrane-bound proteases from preparations of the midgut of 5th instar velvetbean caterpillars, Anticarsia gemmatalis
(Hübner) were obtained by resuspension of the pellet obtained after 100,000 g centrifugation. As expected of trypsin-like proteases,
they hydrolyzed casein and the synthetic substrates N--benzoyl-L-Arg-p-nitroanilidine (L-BApNA) and N--p-tosyl-L-Arg methyl
ester (L-TAME). Higher activities were observed at 50°C, and at pH 8.5 and 8.0 for both synthetic substrates L-BApNA and
L-TAME. The membrane-bound proteases were inhibited by EDTA, phenylmethan sulphonyl fluoride (PMSF), tosyl-L-lysine chloromethyl
ketone (TLCK), benzamidine and aprotinin. TLCK and benzamidine were particularly active inhibitors. The KM-values
obtained were 0.23 mM for L-BApNA and 92.5 μM for L-TAME. These results provide evidence for the presence of membranebound
trypsin-like proteases in the midgut of the velvetbean caterpillar, a key soybean pest in warm climates. The interaction
between A. gemmatalis digestive proteases and soybean protease inhibitors has potentially important consequences for soybean
breeding programs. | pt_BR |
Affilliation | Universidade Federal de Viçosa. Instituto de Biotecnologia Aplicada à Agricultura e Ciência Animal. Departamento de Bioquímica e Biologia Molecular. Viçosa, MG, Brasil. | pt_BR |
Affilliation | Universidade Federal de Viçosa. Instituto de Biotecnologia Aplicada à Agricultura e Ciência Animal. Departamento de Bioquímica e Biologia Molecular. Viçosa, MG, Brasil / Universidade Federal de Viçosa. Departamento de Biologia Animal. Viçosa, MG, Brasil. | pt_BR |
Affilliation | Universidade Federal de Viçosa. Departamento de Biologia Animal. Viçosa, MG, Brasil. | pt_BR |
Affilliation | Universidade Federal de Viçosa. Departamento de Microbiologia. Instituto de Biotecnologia Aplicada à Agricultura e Ciência Animal. Departamento de Bioquímica e Biologia Molecular. Viçosa, MG, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil. | pt_BR |
Subject | Trypsin | pt_BR |
Subject | Proteases | pt_BR |
Subject | Velvetbean caterpillar | pt_BR |
Subject | Lepidoptera | pt_BR |
Subject | Noctuidae | pt_BR |
Subject | Anticarsia | pt_BR |