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

Abstract

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.

Lactose and Galactose Promote the Crystallization of Human Galectin-10

“…The monomer–dimer equilibrium was also determined by native polyacrylamide gel electrophoresis (PAGE) [ 55 ]. Gal-10 was diluted to 10 μM and incubated with or without 1 mM lactose, galactose, sucrose, or glucose for 2 h. After the native PAGE, the gel was stained with Coomassie Blue R-250.…”