Purification and erythrocyte-membrane perturbing activity of a ketose-specific lectin from Moringa oleifera seeds

Abstract

Highlights Purification of Moringa oleifera seed lectin (MoL) was achieved by ammonium sulfate precipitation and size exclusion chromatography MoL hemagglutinating activity was thermostable up to 90°C, within pH 2-4 and moderately inhibited by sucrose and fructose Traces of Ca2+, Mg2+, and Na+ was detected in MoL, and modification of arginine and tryptophan residues affected the hemagglutinating activity Hemolytic (membrane-perturbing) activity of MoL was potentiated in mildly acidic pH, and dependent on concentration, temperature, pH, and time of incubation.

Purification, Partial Characterization, and Evaluation of the Antiulcer Activity of Calotropis procera Leaf Lectin

“…Oxidation of exposed tryptophan at low pH is often done by the tryptophan-specific reagent N-bromosuccinimide (NBS) [ 37 , 38 ]. Titration of ProLec with aliquots of NBS at pH 6, indicated that exposed tryptophan residues represented approx 2% of the total protein (Figure 5 ), and modification of half of these tryptophans residues inactivated protein (results not shown).…”

Antimicrobial Activities and Phylogenetic Study of Erythrina senegalensis DC (Fabaceae) Seed lectin

“…Purification was repeated several times to obtain pure ESL in sufficient quantities for antimicrobial study. The purity and molecular weight of ESL were determined using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) on a 12.5% acrylamide gel using low-molecular-weight protein markers (Nubi et al, 2021 ).…”

“…Lectins are unique proteins or glycoproteins, having at least one domain devoid of catalytic activity and capable of binding specific glycan moieties reversibly (Alen’kina et al, 2014 ; Nubi et al, 2021 ). These proteins are heterogeneous in structures and proficient in agglutinating or precipitating cells and carbohydrate-relate structures via specific interactions (Singh et al, 2016 ; Adedoyin et al, 2021 ).…”