Lectins are non-immune carbohydrate-binding proteins/glycoproteins that are found everywhere in nature, from bacteria to human cells. They have also been a valuable biological tool for the purification and subsequent characterisation of glycoproteins due to their carbohydrate binding recognition capacity. Antinociceptive, antiulcer, anti-inflammatory activities and immune modulatory properties have been discovered in several plant lectins, with these qualities varying depending on the lectin carbohydrate-binding site.
View Article and Find Full Text PDFLectins are proteins or glycoproteins that bind specifically and reversibly to the carbohydrate or glycoconjugates. A new lectin is purified from the rhizome of Xanthosoma violaceum Schott. by successive steps of ammonium sulfate fractionation and affinity chromatography with asialofetuin as ligand.
View Article and Find Full Text PDFUnlabelled: Plant lectins are carbohydrate-binding proteins that are ubiquitously found in almost all plant species and have different structures and functions depending on the sources. Purifying lectins from their plant sources and determining their sugar specificity become an important goal for evaluating their potential biomedical applications. Here, we report the affinity purification of a Dgalactose specific lectin from the seeds of Meizotropis buteiformis Voigt.
View Article and Find Full Text PDFCurr Protein Pept Sci
August 2019
Lectins are proteins or glycoproteins of non-immune origin which have at least one noncatalytic domain that bind reversibly to specific mono or oligosaccharides. Traditional Chinese Medicine (TCM) involves a broad range of medicinal practices sharing common concepts which have been developed in China and are based on a tradition of more than thousands of years. Plant materials which are commonly used in TCM as a complementary or alternative for Western medical treatments contain a considerable number of important lectins.
View Article and Find Full Text PDFThe innate immune system plays a modulatory role in producing an inflammatory response during microbial infection and tissue regeneration. Mannose-binding lectin (MBL) is a predominant constituent of the innate immune system which initiates one of the complement activation, the lectin pathway. The activation of the complement system is also associated with many human diseases.
View Article and Find Full Text PDFLectins including flowering plant lectins, algal lectins, cyanobacterial lectins, actinomycete lectin, worm lectins, and the nonpeptidic lectin mimics pradimicins and benanomicins, exhibit anti-HIV activity. The anti-HIV plant lectins include Artocarpus heterophyllus (jacalin) lectin, concanavalin A, Galanthus nivalis (snowdrop) agglutinin-related lectins, Musa acuminata (banana) lectin, Myrianthus holstii lectin, Narcissus pseudonarcissus lectin, and Urtica diocia agglutinin. The anti-HIV algal lectins comprise Boodlea coacta lectin, Griffithsin, Oscillatoria agardhii agglutinin.
View Article and Find Full Text PDFMushrooms are famous for their nutritional and medicinal values and also for the diversity of bioactive compounds they contain including lectins. The present review is an attempt to summarize and discuss data available on molecular weights, structures, biological properties, N-terminal sequences and possible applications of lectins from edible mushrooms. It further aims to update and discuss/examine the recent advancements in the study of these lectins regarding their structures, functions, and exploitable properties.
View Article and Find Full Text PDFLectins are a group of proteins of non-immune origin that recognize and bind to carbohydrates without modifying them. Banana is the common name for both herbaceous plants of the genus Musa and for the fruit they produce. They are indeed a promising source for many medicinal applications.
View Article and Find Full Text PDFA new magnesium ion requiring N-acetyl-D-glucosamine specific lectin QIL was purified to electrophoretic homogeneity from seeds of Quercus ilex L. through successive steps of (i) lectin extraction, (ii) ammonium sulphate (30-50%) fractionation, (iii) diethylaminoethyl (DEAE)-cellulose chromatography, (iv) carboxymethyl (CM)-cellulose chromatography, and (v) Sephadex G-75 chromatography. The lectin, having specific activity of 25,600 hemagglutination units (HAU)/mg of protein, was found to be a monomeric protein with a native molecular weight of 13.
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