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Macromolecular Properties of Diocleinae Lectins

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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: C. ensisformis; C. maritime; Canavalia brasiliensis; Canavalia ensiformis; Canavalia maritima; Cratylia floribunda; D.virgata; DIOCLEINAE LECTINS; Dioclea grandiflora; Diolcea grandiflora

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866013409193

Affiliations: Departamento de Biologia and 3Bioquimica e Biologia Molecular, Universidade Federal do Ceara, Caixa Postal 6033, CEP 60451-970. Fortaleza-Ceara, Brasil.

Publication date: October 1, 2001

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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