Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds

Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds

Autor Mello, G. C. Google Scholar
Oliva, MLV Google Scholar
Sumikawa, J. T. Google Scholar
Machado, OLT Google Scholar
Marangoni, S. Google Scholar
Novello, J. C. Google Scholar
Macedo, MLR Google Scholar
Instituição Universidade Federal de Mato Grosso do Sul (UFMS)
Universidade Estadual de Campinas (UNICAMP)
Universidade Federal de São Paulo (UNIFESP)
Univ Estadual Norte Fluminense
Resumo 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.
Palavra-chave Dimorphandra mollis
Mimosoideae
trypsin inhibitor
N-terminal sequence
Kunitz family
Idioma Inglês
Data de publicação 2001-11-01
Publicado em Journal of Protein Chemistry. New York: Kluwer Academic/plenum Publ, v. 20, n. 8, p. 625-632, 2001.
ISSN 0277-8033 (Sherpa/Romeo, fator de impacto)
Publicador Kluwer Academic/plenum Publ
Extensão 625-632
Fonte http://dx.doi.org/10.1023/A:1013764118579
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000174160400005
Endereço permanente http://repositorio.unifesp.br/handle/11600/26659

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