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Type: Artigo de periódico
Title: Novel protein from Labramia bojeri A. DC. seeds homologue to Kunitz-type trypsin inhibitor with lectin-like properties
Author: Macedo, MLR
Freire, MDM
Martins, LTDM
Martinez, DST
Gomes, VM
Smolka, MB
Toyama, MH
Marangoni, S
Coelho, LCBB
Abstract: This study starts by isolating and characterizing the first protein from Labramia bojeri seeds, which belong to the Sapotaceae family. The purified lectin analyzed by SIDS-PAGE with and without beta-mercaptoethanol shows two protein bands (M-r = 19 and 20 kDa), which cannot be resolved. Protein bands have shown similar characteristics as molecular masses, determined by gel filtration and native gel; N-terminal sequences presented a difference in their isoelectric points. We have suggested that those protein bands might be variants of the protein named Labramin. The sequence database search has shown that the N-terminal sequence of Labramin presented a high degree of homology to Kunitz-type trypsin inhibitor (82-52%) despite no trypsin inhibition activity detection. The lectin-like form from Labramin was better inhibited by glycoproteins and has also presented growth inhibition of the fungus Colletotrichum lindemuthianum and the yeast Saccharomyces cerevisiae, but it has not presented an apparent effect on Fusarium oxysporum.
Subject: Labramia bojeri
trypsin inhibitor
Colletotrichum lindemuthianum
Saccharomyces cerevisiae
Country: EUA
Editor: Amer Chemical Soc
Citation: Journal Of Agricultural And Food Chemistry. Amer Chemical Soc, v. 52, n. 25, n. 7548, n. 7554, 2004.
Rights: fechado
Identifier DOI: 10.1021/jf048535p
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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