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Purification and Biochemical Characterization of a Protease Inhibitor Ⅱ Family from Jalapeno Pepper(Capsicum annuum L.)
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作者 Juan Pablo Carrillo-Montes Roberto Arreguin-Espinosa +1 位作者 Jose Luis Munoz-Sanchez Manuel Soriano-Garcia 《Advances in Bioscience and Biotechnology》 2014年第7期661-668,共8页
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... 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 jalape&ntildeo 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. 展开更多
关键词 protease inhibitory activity protease Inhibitor Protein Purification Jalapeno Pepper Capsicum annuum L.
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