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

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...

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Veröffentlicht in:	Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2004-05, Vol.138 (1), p.81-89
Hauptverfasser:	Aguirre, Cesar, Valdés-Rodrı́guez, Silvia, Mendoza-Hernández, Guillermo, Rojo-Domı́nguez, Arturo, Blanco-Labra, Alejandro
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Bostrichidae Chan Chromatography, Liquid Circular Dichroism Coleoptera - drug effects Coleoptera - enzymology Hydrogen-Ion Concentration Hyptis suaveolens Isoelectric Point Lamiaceae - chemistry Larger grain borer Maize Manduca sexta Molecular Weight Peptide Hydrolases - metabolism Plant defense mechanisms Prostephanus truncatus Protease inhibitor Protease Inhibitors - chemistry Protease Inhibitors - isolation & purification Protease Inhibitors - pharmacology Proteases Protein Denaturation Seeds - chemistry Temperature Zea mays - parasitology
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