Defining a lectin

Kocourek, J.; Hořejšı́, Václav

doi:10.1038/290188a0

Cited by 79 publications

(18 citation statements)

References 2 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lectins are glycoproteins of non-immune origin which specifically and reversibly bind carbohydrates, producing agglutination of cells and precipitate polysaccharides and glycoproteins, due to the presence of at least one non-catalytic domain [1][2][3]. Although lectins are present in most living organisms, plant lectins is the most investigated group [4].…”

Section: Introductionmentioning

confidence: 99%

Characterization of Two Non-Fetuin-Binding Lectins from Tepary Bean (Phaseolus acutifolius) Seeds with Differential Cytotoxicity on Colon Cancer Cells

Arteaga¹,

Guillen²

2016

J Glycobiol

View full text Add to dashboard Cite

Two non-fetuin-binding lectins from tepary bean (Phaseolus acutifolius) seeds were purified and characterized. Both lectins LA and LB showed by two dimensional gel electrophoresis very similar apparent molecular mass, and their isoelectric point for both lectins were also very close. Mass spectrometry analysis confirmed these similarities showing high sequence homology among them, and when these sequences were compared to the Mirkov´s deduced sequence of the phyto-hemagglutinin from Phaseolus acutifolius, LA showed higher homology than LB. On the other hand, when their biological activity was determined, only LA possessed affinity to type A erythrocytes, and when these lectins using a semi pure fraction were measured for their cytotoxic effect on colon cancer cells, they showed a differential effect. In the semi pure protein fraction tested, the rest of no-lectin proteins separated by electrophoresis presented no activity. Our results indicate that despite the high homology in their sequence, isoelectric point, and apparent molecular mass, these two structurally closely related lectins, showed differences in their biological behaviour, represented by their agglutinatination activity, as well as, in their cytotoxic effect on human colon cancer cells.

show abstract

Section: Introductionmentioning

confidence: 99%

Characterization of Two Non-Fetuin-Binding Lectins from Tepary Bean (Phaseolus acutifolius) Seeds with Differential Cytotoxicity on Colon Cancer Cells

Arteaga¹,

Guillen²

2016

J Glycobiol

View full text Add to dashboard Cite

show abstract

“…Lectinlike protein have been found to appear in the Leguminosa Dolichos biflorus on wounding and after a heat shock [Etzler 1996]. These results relativize the classical definition of lectins as constitutive proteins that do not need an external stimulus to be expressed [Goldstein et al, 1980;Kocourek and Horejsi, 1980].…”

Section: Occurrence Localization and Biosynthesismentioning

confidence: 57%

Plant Lectins – More than Just Tools for Glycoscientists: Occurrence, Structure, and Possible Functions of Plant Lectins

Rüdiger¹

1998

Cells Tissues Organs

View full text Add to dashboard Cite

show abstract

“…Lectins are natural proteins characterized by their ability to selectively bind carbohydrate ligands. Most lectins bind reversibly, do not modify carbohydrate covalent structures, and are non-immune in origin [175]. Hundreds of lectins have been described and more than 60 are commercially available, with specificity ranging from very broad (e.g.…”

Section: Glycoproteomicsmentioning

confidence: 99%

Advances in purification and separation of posttranslationally modified proteins

Černý

Skalák

Cerná

et al. 2013

Journal of Proteomics

View full text Add to dashboard Cite

Posttranslational modifications (PTMs) of proteins represent fascinating extensions of the dynamic complexity of living cells' proteomes. The results of enzymatically catalyzed or spontaneous chemical reactions, PTMs form a fourth tier in the gene -transcript -protein cascade, and contribute not only to proteins' biological functions, but also to challenges in their analysis. There have been tremendous advances in proteomics during the last decade. Identification and mapping of PTMs in proteins have improved dramatically, mainly due to constant increases in the sensitivity, speed, accuracy and resolution of mass spectrometry (MS). However, it is also becoming increasingly evident that simple gel-free shotgun MS profiling is unlikely to suffice for comprehensive detection and characterization of proteins and/or protein modifications present in low amounts. Here, we review current approaches for enriching and separating posttranslationally modified proteins, and their MS-independent detection. First, we discuss general approaches for proteome separation, fractionation and enrichment. We then consider the commonest forms of PTMs (phosphorylation, glycosylation and glycation, lipidation, methylation, acetylation, deamidation, ubiquitination and various redox modifications), and the best available methods for detecting and purifying proteins carrying these PTMs.

show abstract

Defining a lectin

Cited by 79 publications

References 2 publications

Characterization of Two Non-Fetuin-Binding Lectins from Tepary Bean (Phaseolus acutifolius) Seeds with Differential Cytotoxicity on Colon Cancer Cells

Characterization of Two Non-Fetuin-Binding Lectins from Tepary Bean (Phaseolus acutifolius) Seeds with Differential Cytotoxicity on Colon Cancer Cells

Plant Lectins – More than Just Tools for Glycoscientists: Occurrence, Structure, and Possible Functions of Plant Lectins

Advances in purification and separation of posttranslationally modified proteins

Contact Info

Product

Resources

About