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

Alberto Caceres Huambo

doi:10.4067/S0718-34292017005000006

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

Translated title of the contribution: 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

Alberto Caceres Huambo

Departamento Académico de Biología

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Translated title of the contribution	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
Original language	Spanish
Pages (from-to)	11-18
Number of pages	8
Journal	Idesia
Volume	35
Issue number	1
DOIs	https://doi.org/10.4067/S0718-34292017005000006
State	Published - Mar 2017

Bibliographical note

Funding Information:
Estudio de homología secuencial de la estructura primaria y construcción del árbol filogenético: La secuencia completa de aminoácidos (estructura primaria), obtenida del paso anterior, fue comparada en relación con el grado de homología con otras secuencias obtenidas del programa SWISS-PROT (Swiss Institute of Bioinformatics), website: http://www.ncbi.nlm.nih.gov. Para la construcción del árbol filogenético o filograma se usó el programa DNASTAR (ClustalW) que permite obtener las distancias nucleotídicas a partir del alineamiento de las secuencias aminoacídicas ingresadas.

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

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title = "Determinaci{\'o}n 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",

abstract = "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.",

keywords = "Amino acid sequence, Antibacterial effect, Lectin, Pisum sativum, Primary structure",

author = "{Caceres Huambo}, Alberto",

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AB - 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.

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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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