Artículos de revistas
Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds
Registro en:
Journal Of Protein Chemistry. Kluwer Academic/plenum Publ, v. 20, n. 8, n. 625, n. 632, 2001.
0277-8033
WOS:000174160400005
10.1023/A:1013764118579
Autor
Mello, GC
Oliva, MLV
Sumikawa, JT
Machado, OLT
Marangoni, S
Novello, JC
Macedo, MLR
Institución
Resumen
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. 20 8 625 632