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|Title:||Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds|
|Authors:||Mello, G. C.|
Sumikawa, J. T.
Novello, J. C.
Universidade Federal de Mato Grosso do Sul (UFMS)
Universidade Estadual de Campinas (UNICAMP)
Universidade Federal de São Paulo (UNIFESP)
Univ Estadual Norte Fluminense
|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.|
|Appears in Collections:||Em verificação - Geral|
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