Macromolecular Properties of Diocleinae Lectins
Authors: Marcio V. Ramos1; Leila M. Beltramini1; Renato A. Moreira1
Source: Protein and Peptide Letters, Volume 8, Number 5, October 2001 , pp. 399-406(8)
Publisher: Bentham Science Publishers
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Abstract:
Structural properties of six closely related lectins isolated from plants belonging from the legume group Diocleinae were studied in solution. Affinity and gel filtration chromatography of the lectins at different pH conditions demonstrated that the lectins diverge in affinity for a specific matrix mainly at the pH range 4.0 up to 6.0 and that at neutral pH they tend to form dimers. Analysis of circular dichroism and fluorescence emission spectra stressed the differences of the lectin from Cratylia floribunda seeds from that of Canavalia brasiliensis, C. ensisformis, C. maritima, Diolcea grandiflora and D.virgata. According to the results, these proteins constitute a excellent model to study fine protein structure / function relationships.Keywords: DIOCLEINAE LECTINS; Cratylia floribunda; Canavalia brasiliensis; C. ensisformis; C. maritime; Diolcea grandiflora; D.virgata; Canavalia ensiformis; Dioclea grandiflora; Canavalia maritima
Document Type: Review article
DOI: 10.2174/0929866013409193
Affiliations: 1: Departamento de Biologia and 3Bioquimica e Biologia Molecular, Universidade Federal do Ceara, Caixa Postal 6033, CEP 60451-970. Fortaleza-Ceara, Brasil.
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