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solanum tuberosum lectin/solanum
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Studies on the chemical modification and potato (Solanum tuberosum) lectin and its effect on haemagglutinating activity.
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1. Modification of potato (Solanum tuberosum) lectin with acetic anhydride blocked 5.1 amino and 2.7 tyrosyl groups per molecule of lectin and decreased the haemagglutinating activity of the lectin. De-O-acetylation regenerated 2.0 of the tyrosyl groups and resulted in a recovery of activity. 2.
The production and properties of an antiserum to potato (Solanum tuberosum) lectin.
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Precipitation of potato (Solanum tuberosum) lectin by antisera was not affected by treatments that abolish lectin activity. An antiserum precipitated glycosylated derivatives of the lectin but not a deglycosylated peptide. The haemagglutination inhibition titre of this antiserum was not affected by
Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism.
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The structure of potato (Solanum tuberosum) lectin, which is a hydroxyproline-rich glycoprotein, has been investigated by circular dichroism. The spectra of the native lectin, and of the oxidized, reduced and carboxymethylated and deglycosylated derivatives were examined, as was a
The properties of potato (Solanum tuberosum) lectin after deglycosylation by trifluoromethanesulphonic acid.
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Potato (Solanum tuberosum) lectin, which is a very highly glycosylated glycoprotein, has been completely deglycosylated by use of the trifluoromethanesulphonic acid reagent described by Edge, Faltnek, Hof, Reichert & Weber [(1981) Analyt. Biochem. 118, 131-137]. This shows that both
Solanum tuberosum lectin-conjugated PLGA nanoparticles for nose-to-brain delivery: in vivo and in vitro evaluations.
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Solanum tuberosum lectin (STL) conjugated poly (DL-lactic-co- glycolic acid) (PLGA) nanoparticle (STL-NP) was constructed in this paper as a novel biodegradable nose-to-brain drug delivery system. The in vitro uptake study showed markedly enhanced endocytosis of STL-NP compared to unmodified PLGA
Lectin-mediated drug targeting: quantification of binding and internalization of Wheat germ agglutinin and Solanum tuberosum lectin using Caco-2 and HT-29 cells.
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For the potential use of Wheat germ agglutinin (WGA) and Solanum tuberosum lectin (STL) as auxiliary excipients for targeting drugs to colonocytes, the number of Caco-2 and HT-29-bound lectins was determined by fluorimetry using fluorescein-labelled derivatives of the N-acetylglucosamine-specific
On the specificity of lectins with a broad agglutination spectrum. I. The nature of the specific receptors for Ricinus communis and Solanum tuberosum Lectins.
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Proceedings: Purification and characterization of potato (Solanum tuberosum) lectin.
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Solanum tuberosum lectin inhibits Ehrlich ascites carcinoma cells growth by inducing apoptosis and G2/M cell cycle arrest.
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Recently, a lectin was purified from the potato cultivated in Bangladesh locally known as Sheel. In the present study cytotoxicity of the lectin against Ehrlich ascites carcinoma (EAC) cells was studied by MTT assay in vitro in RPMI-1640 medium and 8.0-36.0 % cell growth inhibition was observed at
Purification of potato lectin (Solanum tuberosum agglutinin) from tubers or fruits using chromatofocusing.
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The lectin from potato tubers (Solanum tuberosum agglutinin) has been purified to homogeneity by a procedure involving chromatofocusing followed by gel filtration. By subjecting tuber and fruit extracts from an individual plant to this purification scheme, it was demonstrated that the lectins from
Structural studies of the carbohydrate moieties of lectins from potato (Solanum tuberosum) tubers and thorn-apple (Datura stramonium) seeds.
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1. Methylation analysis of potato (Solanum tuberosum) lectin and thorn-apple (Datura stramonium) lectin confirmed previous conclusions that both glycoproteins contained high proportions of l-arabinofuranosides and lesser amounts of d-galactopyranosides. The arabinofuranosides are present in both
A rapid and effective method for purification of a heat-resistant lectin from potato (Solanum tuberosum) tubers.
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The potato lectin has been identified to consist of two chitin-binding modules, each containing twin hevein domains. Based on the thermotolerance of the hevein polypeptide, a simple, rapid, and effective protocol for the small-scale purification of the potato lectin has been developed in this study.
Purification of a novel chitin-binding lectin with antimicrobial and antibiofilm activities from a bangladeshi cultivar of potato (Solanum tuberosum).
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A new chitin-binding lectin was purified from a Bangladeshi cultivar 'Deshi' of potato (Solanum tuberosum L.) through anion-exchange and affinity chromatographies using a chitin column. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) showed the molecular mass of the lectin as
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