Topic
Isolectins
About: Isolectins is a research topic. Over the lifetime, 169 publications have been published within this topic receiving 4338 citations.
Papers published on a yearly basis
Papers
TL;DR: The purification of wheat-germ agglutinin from commercial wheat germ is described and it is proposed that the binding site consists of three or four subsites with differing specificities, in a cleft in the molecule resembling that for hen's-egg-white lysozyme.
Abstract: 1 The purification of wheat-germ agglutinin from commercial wheat germ is described By ion-exchange chromatography three active proteins (isolectins) were separated, one of which was examined in detail 2 The amino acid composition is unusual, as 20% of residues are half-cystine and 21% are glycine Unlike most lectins and contrary to previous reports, this protein is not a glycoprotein 3 The efficiency of various saccharides as inhibitors of the agglutination reaction was investigated and from this the specificity of the binding site was inferred Of monosaccharides, only derivatives of glucose with a 2-acetamido group and a free 3-hydroxyl group are effective inhibitors, and glycosides of either anomeric configuration are bound Oligosaccharides are much more powerful inhibitors of agglutination than are monosaccharides 4 It is proposed that the binding site consists of three or four subsites with differing specificities, in a cleft in the molecule resembling that proposed for hen9s-egg-white lysozyme
590 citations
TL;DR: Affinity-purified phytohemagglutinin from red kidney bean resolves into five isolectins by SP-Sephadex ion exchange chromatography that are homogeneous by ultracentrifugation and suggest tetrameric quaternary structures.
221 citations
TL;DR: The results of fractionation studies and chemical, physical and immunochemical investigations established the existence of a range of closely related glycoproteins in the albumin fraction of the seeds of “haricot” kidney bean, shown to be agglutinins, or isolectins, of red or white blood cells.
107 citations
TL;DR: Two noteworthy features of WGA specificity emerge from an examination of the observed affinities: (1) both isolectins bind the alpha (2,3) isomer of N-acetylneuraminyllactose with higher affinity than the alpha(2,6) form and (2) WGA I binds two of the sialyloligosaccharides more tightly than does WGA II.
Abstract: The binding of three purified sialic acid containing oligosaccharides to two isolectins of wheat germ agglutinin (WGA I and WGA II) has been quantitated by measuring the broadening of a ligand resonance in the proton nuclear magnetic resonance (1H NMR) spectrum at 360 MHz. The ligands, isolated from bovine colostrum by using the procedure of Schneir and Rafelson [Schneir, M. L., & Rafelson, M. E., Jr. (1966) Biochim. Biophys, Acta 130, 1--11], were identified by 1H NMR as the alpha (2,3) and alpha (2,6) isomers of N-acetylneuraminyllactose, as well as the alpha (2,6) form of N,N'-diacetylneuraminyllactosamine. The dissociation constants, KD's, ranged from 0.7 to 10 mM (24 +/- 1 degree C). Two noteworthy features of WGA specificity emerge from an examination of the observed affinities: (1) both isolectins bind the alpha (2,3) isomer of N-acetylneuraminyllactose with higher affinity than the alpha (2,6) form and (2) WGA I binds two of the sialyloligosaccharides more tightly than does WGA II.
100 citations
TL;DR: Comparison of the primary structures between the vertebrate 14-kDa-type lectins suggests that C-14 and C-16 were produced by gene duplication of an ancestral lectin gene at a time close to the divergence of birds and mammals.
85 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2020 | 4 |
| 2019 | 1 |
| 2018 | 1 |
| 2017 | 2 |
| 2016 | 1 |
| 2015 | 5 |