Trypsin inhibitor from Dimorphandra mollis seeds: purification and properties |
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Authors: | Macedo M L de Matos D G Machado O L Marangoni S Novello J C |
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Affiliation: | Departamento de Ciências Naturais, Universidade Federal de Mato Grosso do Sul, Três Lagoas, Brazil. bioplant@bestway.com.br |
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Abstract: | A trypsin inhibitor from Dimorphandra mollis seeds was isolated to apparent homogeneity by a combination of ammonium sulfate precipitation, gel filtration, ion-exchange and affinity chromatographic techniques. SDS-PAGE analysis gave an apparent molecular weight of 20 kDa, and isoelectric focusing analysis demonstrated the presence of three isoforms. The partial N-terminal amino acid sequence of the purified protein showed a high degree of homology with various members of the Kunitz family of inhibitors. This inhibitor, which inhibited trypsin activity with a Ki of 5.3 x 10(-10) M, is formed by a single polypeptide chain with an arginine residue in the reactive site. |
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