Partial Characterization of Lectins Purified from the Surco and Vara (Furrow and Rod) Varieties of Black Phaseolus vulgaris .

Autor: Valadez-Vega C; Área Académica de Medicina, Instituto de Ciencias de la Salud, Universidad Autónoma del Estado de Hidalgo, Ex-Hacienda de la Concepción, Tilcuautla, San Agustín Tlaxiaca 42080, Mexico., Lugo-Magaña O; Preparatoria Número 1, Universidad Autónoma del Estado de Hidalgo, Av. Benito Juárez S/N, Constitución, Pachuca de Soto 42060, Mexico., Betanzos-Cabrera G; Área Académica de Nutrición, Instituto de Ciencias de la Salud, Universidad Autónoma del Estado de Hidalgo, Ex-Hacienda de la Concepción, Tilcuautla, San Agustín Tlaxiaca 42080, Mexico., Villagómez-Ibarra JR; Área Académica de Química, Instituto de Ciencias Básicas e Ingeniería, Universidad Autónoma del Estado del Hidalgo, Ciudad del Conocimiento, Mineral de la Reforma 42184, Mexico.
Jazyk: angličtina
Zdroj: Molecules (Basel, Switzerland) [Molecules] 2022 Dec 02; Vol. 27 (23). Date of Electronic Publication: 2022 Dec 02.
DOI: 10.3390/molecules27238436
Abstrakt: As they manifest specifically and reversibly, lectins are proteins or glycoproteins with the characteristic of agglutinating erythrocytes. Given that grain legume lectins can represent 10% of protein content and can have various biological functions, they are extensively studied. The objective of this work was to purify and partially characterize the lectins of Phaseolus vulgaris black, var surco and vara (LBBS and LBBV). Both lectin types were purified by affinity chromatography on stroma matrix, which agglutinated human erythrocytes type A, B, and O, as well as rabbit, hamster, pig, and chicken erythrocytes. Native-PAGE was employed for molecular mass determination, yielding 109.36 and 112.68 kDa for BBS and BBV, respectively. Further analyses revealed that these lectins are tetrameric glycoproteins that require Ca +2 , Mn +2 and Mg +2 ions for exhibiting their hemagglutinating function, which can be inhibited by fetuin. Moreover, optimal pH was established for both lectins (10.5 for LBBS and 7-9 for LBBV), while their activity was temperature-dependent and ceased above 70 °C. Finally, the observed differences in the biochemical characteristics and bioactive functions were ascribed to the different physiological characteristics of each seed, as well as the protein itself.
Databáze: MEDLINE
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