A novel 8.7 kDa protease inhibitor from chan seeds (Hyptis suaveolens L.) inhibits proteases from the larger grain borer Prostephanus truncatus (Coleoptera: Bostrichidae).

نویسندگان

  • Cesar Aguirre
  • Silvia Valdés-Rodríguez
  • Guillermo Mendoza-Hernández
  • Arturo Rojo-Domínguez
  • Alejandro Blanco-Labra
چکیده

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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عنوان ژورنال:
  • Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology

دوره 138 1  شماره 

صفحات  -

تاریخ انتشار 2004