A novel 8.7 kDa protease inhibitor from chan seeds (Hyptis suaveolens L.) inhibits proteases from the larger grain borer Prostephanus truncatus (Coleoptera: Bostrichidae) |
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Authors: | Aguirre Cesar Valdés-Rodríguez Silvia Mendoza-Hernández Guillermo Rojo-Domínguez Arturo Blanco-Labra Alejandro |
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Institution: | Departamento de Biotecnología y Bioquímica, Centro de Investigación y de Estudios Avanzados (Cinvestav) Unidad Irapuato. Km 9.6 Libramiento Norte Carretera Irapuato-León, C.P. 36500 Irapuato Gto, Mexico. |
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Abstract: | A novel trypsin inhibitor purified from chan seeds (Hyptis suaveolens, Lamiaceae) was purified and characterized. Its apparent molecular mass was 8700 Da with an isoelectric point of 3.4. Its N-terminal sequence showed a high content of acidic amino acids (seven out of 18 residues). Its inhibitory activity was potent toward all trypsin-like proteases extracted from the gut of the insect Prostephanus truncatus (Coleoptera: Bostrichidae), a very important pest of maize. This activity was highly specific, because among proteases from seven different insects, only those from P. truncatus and Manduca sexta (Lepidoptera: Sphingidae) were inhibited. This inhibitor has potential to enhance the defense mechanism of maize against the attack of P. truncatus. |
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