Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/95214
Type: Artigo de periódico
Title: Purification And Characterization Of A New Trypsin Inhibitor From Dimorphandra Mollis Seeds
Author: Mello G.C.
Oliva M.L.V.
Sumikawa J.T.
Machado O.L.T.
Marangoni S.
Novelle J.C.
Macedo M.L.R.
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 ionexchange 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 ́ 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. ©2002 Plenum Publishing Corporation.
Editor: 
Rights: fechado
Identifier DOI: 
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-52549129360&partnerID=40&md5=d992f6ac949f1fa5777841233b5d0c18
Date Issue: 2001
Appears in Collections:Unicamp - Artigos e Outros Documentos

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