Determinación de la estructura primaria de la lectina V-2 de semillas de arveja (Pisum sativum L.) y su efecto antibacteriano en Staphylococcus aureus y Escherichia coli

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Resumen

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 a phylogenetic 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.

Título traducido de la contribuciónDetermination 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
Idioma originalEspañol
Páginas (desde-hasta)11-18
Número de páginas8
PublicaciónIdesia
Volumen35
N.º1
DOI
EstadoPublicada - mar. 2017

Nota bibliográfica

Publisher Copyright:
© 2017, Universidad de Tarapaca. All rights reserved.

Palabras clave

  • Amino acid sequence
  • Antibacterial effect
  • Lectin
  • Pisum sativum
  • Primary structure

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