Serine protease inhibitors from Amazon leguminosae seeds: purification and preliminary characterization of two chymotrypsin inhibitors from Inga umbratica

Authors: Calderon A.L.; Teles R.C.L.; Leite J.R.S.A; Bloch J.C.; Astolfi-Filho S.; Freitas M.S.

Source: Protein and Peptide Letters, Volume 8, Number 6, December 2001 , pp. 485-493(9)

Publisher: Bentham Science Publishers

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Abstract:

Nine species of Leguminosae seeds from Amazon forest have been screened for trypsin and chymotrypsin inhibitory activity. The species involved were Cassia basselari, Cassia grandis, Cassia occidentalis, Dialium guianense, Inga fagifolia, Inga rubiginosa, Inga umbratica, Inga velutina and Mimosa guillandinae. Extracts from all the species, except I. umbratica, contained significant activity against trypsin, chymotrypsin and blood human clotting factors Xa. Two new chymotrypsin inhibitors (IuCI-1 and IuCI-2) have been purified to homogeneity from I. umbratica with molecular masses of 20,088.6 and 20,271.2, respectively.

Keywords: Serine protease inhibitors; Inga umbratica; chymotrypsin inhibitory activity; Cassia basselari; Cassia grandis; Cassia occidentalis; Dialium guianense; Inga fagifolia

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409175

Publication date: 2001-12-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.