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1.
Plant Physiol Biochem ; 51: 145-52, 2012 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-22153251

RESUMO

This study aimed to evaluated the resistance and susceptibility of 10 cowpea cultivars to Meloidogyne incognita in field studies and to analyze the kinetics of the enzymes superoxide dismutase, catalase, peroxidase, chitinase, ß-1,3-glucanases and cystein proteinase inhibitors in the root system of two contrasting cowpea cultivars after inoculation with M. incognita. The cultivars CE-31 and Frade Preto were highly resistant; CE-28, CE-01, CE-315, CE-237, were very resistant; CE-70 and CE-216 were moderately resistant, whereas Vita-3 and CE-109 were slightly resistant. In the roots of the highly resistant cultivar CE-31 the activity of the antioxidant enzyme superoxide dismutase increased and catalase decreased and those of the pathogenesis-related proteins chitinase, ß-1,3-glucanase, peroxidase and cystein proteinase inhibitor increased in comparison with the root system of the slightly resistant CE-109, during the course of M. incognita infestation. Thus the changes in the activities of these enzymes might be related to the smaller final population of M. incognita in CE-31 and may contribute to the high resistance of this cowpea cultivar against infection and colonization by this nematode species.


Assuntos
Antioxidantes/metabolismo , Fabaceae/enzimologia , Interações Hospedeiro-Parasita , Proteínas de Plantas/metabolismo , Raízes de Plantas/parasitologia , Tylenchoidea/patogenicidade , Animais , Inibidores de Cisteína Proteinase/metabolismo , Resistência à Doença , Ativação Enzimática , Fabaceae/imunologia , Fabaceae/parasitologia , Feminino , Glucana 1,3-beta-Glucosidase/metabolismo , Infecções por Nematoides/imunologia , Infecções por Nematoides/parasitologia , Peroxidase/metabolismo , Doenças das Plantas/imunologia , Doenças das Plantas/parasitologia , Raízes de Plantas/enzimologia , Raízes de Plantas/imunologia , Especificidade da Espécie , Superóxido Dismutase/metabolismo , Tylenchoidea/imunologia
2.
J Agric Food Chem ; 55(2): 260-6, 2007 Jan 24.
Artigo em Inglês | MEDLINE | ID: mdl-17227051

RESUMO

Chitin-binding vicilin from Enterolobium contortisiliquum seeds was purified by ammonium sulfate followed by gel filtration on Sephacryl 300-SH and on Sephacryl 200-SH. The vicilin, called EcV, is a dimeric glycoprotein composed of 1.03% carbohydrates and a Mr of 151 kDa, consisting of two subunits of Mr of 66.2 and 63.8 kDa. The EcV homogeneity was confirmed in a PAGE where it was observed to be a unique acid protein band with slow mobility in this native gel. E. contortisiliquum vicilin (EcV) was tested for anti-insect activity against C. maculatus and Zabrotes subfasciatus larvae and for phytopathogenic fungi, F. solani and C. lindemuntianum. EcV was very effective against both bruchids, producing 50% mortality for Z. subfasciatus at an LD50 of 0.43% and affected 50% of the larvae mass with an ED50 of 0.65%. In artificial diets given to C. maculatus, 50% of the larvae mass was affected with an ED50 of 1.03%, and larva mortality was 50% at LD50 of 1.11%. EcV was not digested by midgut homogenates of C. maculatus and Z. Subfasciatus until 12 h of incubation, and at 24 h EcV was more resistant to Z. subfasciatus larval proteases. The binding to chitin present in larvae gut associated to low EcV digestibility could explain its lethal effects. EcV also exerted an inhibitory effect on the germination of F. solani at concentrations of 10 and 20 microg mL-1. The effect of EcV on fungi is possibly due to binding to chitin-containing structures of the fungal cell wall.


Assuntos
Quitina/metabolismo , Fabaceae/química , Fungicidas Industriais/farmacologia , Inseticidas , Proteínas de Plantas/farmacologia , Sementes/química , Animais , Besouros , Fungicidas Industriais/isolamento & purificação , Inseticidas/isolamento & purificação , Proteínas de Plantas/isolamento & purificação , Proteínas de Armazenamento de Sementes
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