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has been cited by the following article:

• TITLE: Purification and Biochemical Characterization of a Protease Inhibitor II Family from Jalapeño Pepper (Capsicum annuum L.)

  AUTHORS: Juan Pablo Carrillo-Montes, Roberto Arreguín-Espinosa, José Luis Muñoz-Sánchez, Manuel Soriano-García

  KEYWORDS: Protease Inhibitory Activity, Protease Inhibitor, Protein Purification, Jalapeño Pepper, Capsicum annuum L.

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.5 No.7, June 27, 2014

  ABSTRACT: Capsicum annuum L. was initially domesticated in Mexico and northern Central America, and represented an ancient Neotropical plant food complex. The purpose of this paper is to report the isolation and purification of a novo-member of a protease inhibitor from jalapeño pepper (Capsicum annuum L.) (PIJP). The molecular weight of PIJP inhibitor is 5.95 kDa with 56 amino acids and 6 Cys residues with high inhibitory activity to trypsin with a Ki value of 95 nM. This inhibitor according to the alignment with homologous from NCBI and Pfam databases is a member of proteinase inhibitors II. It is worthwhile to mention a major compositional difference between the proteinase inhibitor II families which have 8 Cys residues. PIJP is the first purified proteinase inhibitor, member of this family with only 6 Cys residues.