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Title: Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds
Authors: Mello, G. C.
Oliva, MLV
Sumikawa, J. T.
Machado, OLT
Marangoni, S.
Novello, J. C.
Macedo, MLR
Universidade Federal de Mato Grosso do Sul (UFMS)
Universidade Estadual de Campinas (UNICAMP)
Universidade Federal de São Paulo (UNIFESP)
Univ Estadual Norte Fluminense
Keywords: Dimorphandra mollis
trypsin inhibitor
N-terminal sequence
Kunitz family
Issue Date: 1-Nov-2001
Publisher: Kluwer Academic/plenum Publ
Citation: Journal of Protein Chemistry. New York: Kluwer Academic/plenum Publ, v. 20, n. 8, p. 625-632, 2001.
Abstract: A second trypsin inhibitor (DMTI-II) was purified from the seed of Dimorphandra mollis (Leguminosae-Mimosoideae) by ammonium sulfate precipitation (30-60%), gel filtration, and ion-exchange and affinity chromatography. A molecular weight of 23 kDa was estimated by gel filtration on a Superdex 75 column SDS-PAGE under reduced conditions showed that DMTI-II consisted of a single polypeptide chain, although isoelectric focusing revealed the presence of three isoforms. the dissociation constant of 1.7 x 10(-9) M with bovine trypsin indicated a high affinity between the inhibitor and this enzyme. the inhibitory activity was stable over a wide pH range and in the presence of DTT. the N-terminal sequence of DMTI-II showed a high degree of homology with other Kunitz-type inhibitors.
ISSN: 0277-8033
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