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Idesia (Arica)

versão On-line ISSN 0718-3429

Resumo

CACERES-HUAMBO, Alberto. Determination of the primary structure of a lectin V-2 from pea (Pisum sativum L.) seeds and his antibacterial effect on Staphylococcus aureus and Escherichia coli. Idesia [online]. 2017, vol.35, n.1, pp.11-18.  Epub 14-Abr-2016. ISSN 0718-3429.  http://dx.doi.org/10.4067/S0718-34292017005000006.

The lectin V-2 from Pisum sativum L. ("arveja") seeds was purified by Sephadex G-75 molecular exclusion chromatography and reverse phase high performance liquid chromatography (RP-HPLC). Two dimensional SDS-PAGE analyses demonstrated that the purified lectin was homogeneous since it appeared as a single protein spot corresponding to ~14 kDa with an isoelectric point of 7.5. Its molecular weight was confirmed by mass spectrometry (MALDI-TOF) to be 14,662.0 Da. The complete amino acid sequence (primary structure) showed that the lectin V-2 contains 128 amino acids. Comparative studies with other lectins show that it has high homology to the lectin from Cratylia mollis L. (91.4%), seeds and continued by the lectin from Cratylia argentea (61.6%) seeds. According to aphylogenetic tree, the lectin V-2 showed an approximation microevolutionary of ~ 1,000 nucleotides with the lectin from C. mollis. Additionally, the lectin V-2 showed antibacterial action on Escherichia coli and Staphylococcus aureus makes an inhibition halo of growth with a concentration of 1 mg.

Palavras-chave : lectin; Pisum sativum; amino acid sequence; primary structure; antibacterial effect.

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