Skip to main content
Springer Nature Link
Log in

Isolation of Plant Lectins

  • Chapter
Lectins and Glycobiology

Part of the book series: Springer Laboratory ((SLM))

  • 228 Accesses

  • 19 Citations

Abstract

Lectins are carbohydrate-binding proteins of nonimmune origin which occur throughout the biosphere (Goldstein and Poretz 1986). Their most obvious property, hemagglutination, has been known for more than a century (Franz 1988), whereas the art of purifying lectins is much younger. The great breakthrough came with the introduction of affinity chromatography, first with homopolymer polysaccharides which are suitable for only certain lectins (Agrawal and Goldstein 1965, 1967), later with tailor-made affinity adsorbents prepared by immobilizing monosaccharides, oligosaccharides, glycopeptides, or glycoproteins to hydrophilic and water-insoluble matrices (Lis and Sharon 1981; Rüdiger 1988). The present chapter deals with the isolation of lectins primarily from plants. The procedures are, however, applicable to lectins from other sources as well.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Similar content being viewed by others

References

  • Agrawal BBL, Goldstein IJ (1965) Specific binding of concanavalin A to cross-linked dextran gels. Biochem J 96, 23C

    Google Scholar 

  • Agrawal BBL, Goldstein IJ (1967) Protein carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross-linked dextran gels. Biochim Biophys Acta 147: 262–271

    PubMed  CAS  Google Scholar 

  • Baues RJ, Gray GR (1977) Lectin purification on affinity columns containing reductively aminated disaccharides. J Biol Chem 252: 57–60

    PubMed  CAS  Google Scholar 

  • Causse H, Lemoin A, Rouge P (1986) Quantification of soybean seed lectin in soybean tissues during the life-cycle of the plant, by an enzyme linked immunosorbent assay (ELISA). In: Bog-Hansen TC, van Driessche E (eds) Lectins—biology, biochemistry, clinical biochemistry Vol 5, p667–675

    Google Scholar 

  • Dean PDG, Johnson WS, Middle FA (1985) Affinity chromatography. A practical approach. IRL Press, Oxford

    Google Scholar 

  • Diaz CL, Lems-van Kan P, van der Schaal I AM, Kijne JW (1984) Determination of pea (Pisum sativum) root lectin using an enzyme-linked immunoassay. Planta 161: 302–307

    Article  CAS  Google Scholar 

  • Felsted RL, Pokrywka G, Chen C, Egorin MJ, Bachur NR (1982) Radioimmunoassay and immunochemistry ofPhaseolus vulgaris phytohemagglutinin: verification of isolectin subunits. Arch Biochem Biophys 215: 89–99

    Article  PubMed  CAS  Google Scholar 

  • Fleischmann G, Rüdiger H (1986) Isolation, resolution and partial characterization of two Robinia pseudo-acacia seed lectins. Biol Chem Hoppe-Seyler 367: 27–32

    Article  PubMed  CAS  Google Scholar 

  • Fleischmann G, Mauder I, lllert W, Rüdiger H (1985) A one-step procedure for isolation and resolution of the Phaseolus vulgaris isolectins by affinity chromatography. Biol Chem Hoppe-Seyler 366: 1029–1032

    Article  PubMed  CAS  Google Scholar 

  • Franz H (1988) The ricin story. Adv Lectin Res Vol 1: 10–25

    Google Scholar 

  • Freier T, Fleischmann G, Rüdiger H (1985) Affinity chromatography on immobilized hog gastric mucin and ovomucoid. A general method for isolation of lectins Biol Chem Hoppe-Seyler 366: 1023–1028

    Article  PubMed  CAS  Google Scholar 

  • Ghosh M, Bachhawat BK, Surolia A (1979) A rapid and sensitive assay for detection of nanogram quantities of castor bean (Ricinus communis) lectins. Biochem J 183: 185–188

    PubMed  CAS  Google Scholar 

  • Goldstein IJ, Poretz RD (1986) Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins. In: Liener IE, Sharon N, Goldstein IJ (eds) The lectins, properties, functions, and applications in biology and medicine Academic Press, New York, p33–247

    Google Scholar 

  • Gray GR (1974) The direct coupling of oligosaccharides to proteins and derivatized gels. Arch Biochem Biophys 163: 426–428

    Article  PubMed  CAS  Google Scholar 

  • Hořejší V, Kocourek J (1973) Studies on phytohemagglutinins. XII. O-Glycosyl Polyacrylamide gels for affinity chromatography of phytohemagglutinins. Biochim Biophys Acta 297: 346–351

    Article  PubMed  Google Scholar 

  • Hořejší V, Kocourek J (1974) O-Glycosyl Polyacrylamide gels: application to phytohemagglutinins. Methods in Enzymol 34: 361–367

    Article  Google Scholar 

  • Hořejší V, Tichä M, Kocourek J (1977) Studies on lectins. XXXI. Determination of dissociation constants of lectin-sugar complexes by means of affinity electrophoresis. Biochim Biophys Acta 499: 290–300

    Article  PubMed  Google Scholar 

  • Hořejší V, Tichä M, Kocourek J (1979) Affinity electophoresis. TIBS 4, N6-N7

    Google Scholar 

  • Jourdian GW, Dean L, Roseman S (1971) The sialic acids. XI. A periodate resorcinol method for the quantitative estimation of free sialic acids and their glycosides. J Biol Chem 246: 430–435

    PubMed  CAS  Google Scholar 

  • Kaku H, Goldstein I J, Oscarson S (1991) Interactions of five D-mannose-specific lectins with a series of synthetic branched trisaccharides. Carbohydr Res 213: 109–116

    Article  PubMed  CAS  Google Scholar 

  • Kaul R, Read J, Mattiasson B (1991) Screening for plant lectins by latex agglutination tests. Phytochemistry 30: 4005–4009

    Article  CAS  Google Scholar 

  • Kohn J, Wilchek M (1982) A new approach (cyano transfer) for cyanogen bromide activation of Sepharose at neutral pH, which yields activated resins, free of interfering nitrogen derivatives Biochem Biophys Res Commun 107: 878–884

    Article  PubMed  CAS  Google Scholar 

  • Kolberg J, Michaelsen TE, Sletten K (1983) Properties of a lectin purified from the seeds of Cicer arietinum. Hoppe-Seyler’s Z physiol Chem 364: 655–664

    Article  PubMed  CAS  Google Scholar 

  • Lauriére M, Lauriere C, Chrispeels MJ, Johnson KD, Sturm A (1989) Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins. Plant Physiol 90: 1182–1188

    Article  PubMed  Google Scholar 

  • Lineweaver H, Murray CW (1947) Identification of the trypsin inhibitor of egg white. J Biol Chem 171: 565–581

    PubMed  CAS  Google Scholar 

  • Lis H, Sharon N (1972) Soy bean (Glycine max) agglutinin. Methods in Enzymol 28: 360–368

    Article  Google Scholar 

  • Lis H, Sharon N (1981) Affinity chromatography for the purification of lectins. J Chromatogr 215: 361–372

    Article  CAS  Google Scholar 

  • Lönngren J, Goldstein I J, By water R (1976) Cross-linked guaran: a versatile immunosorbent for D-galactopyranosyl binding lectins. FEBS Letters 68: 31–34

    Article  PubMed  Google Scholar 

  • Loomis WD, Bataille J (1966) Plant phenolic compounds and the isolation of plant enzymes. Phytochemistry 5, 423–438

    Article  CAS  Google Scholar 

  • Luck K, Ehwald R, Ziska P, Koppitz H (1992) Affinity sorbent for galactose-specific lectins consisting of deproteinized plant cell wall ghost. Plant sci 82: 29–35

    Article  CAS  Google Scholar 

  • Nilsson B, Larsson AC, Pählsson K, Öhgren Y, Back M, Nilsson K (1988) An amplification technology for improving sensitivity when measuring components in biological samples. J Immunol Methods 108: 237–244

    Article  PubMed  CAS  Google Scholar 

  • Pongor S, Riedl Z (1983) A latex agglutination test for lectin binding. Anal Biochem 129: 51–56

    Article  PubMed  CAS  Google Scholar 

  • Porath J (1974) General methods and coupling procedures. Affinity chromatography. Methods in Enzymol 34: 13–30

    Article  CAS  Google Scholar 

  • Ramakrishnan R, Eagle MR, Houston LL (1982) RIA of ricin A- and B-chain applied to samples of ricin A-chain prepared by chromatofocussing and by DEAE Bio-Gel A chromatography. Biochim Biophys Acta 719: 341–348

    Article  PubMed  CAS  Google Scholar 

  • Rüdiger H (1988) Preparation of plant lectins. In: Franz H (ed) Adv Lectin Res Vol 1, p26–72

    Google Scholar 

  • Scatchard G (1949) The attraction of proteins for small molecules and ions Ann N Y Acad sci 51: 660–672

    Article  CAS  Google Scholar 

  • Schlumbaum A, Mauch F, Vögeli U, Boller T (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365–367

    Article  CAS  Google Scholar 

  • Schurz H, Rüdiger H (1982) A spectrophotometric determination of protein immobilized to affinity gels. Anal Biochem 123: 174–177

    Article  PubMed  CAS  Google Scholar 

  • Scopes R (1982) Protein purification. Principles and practice. Springer, New York Heidelberg Berlin

    Google Scholar 

  • So LL, Goldstein IJ (1967) Protein-carbohydrate interaction. IV. Application of the quantitative precipitin method to polysaccharide-concanavalin A interaction. J Biol Chem 242: 1617–1622

    PubMed  CAS  Google Scholar 

  • So LL, Goldstein IJ (1968) Protein-carbohydrate interaction. XIII. The interaction of concanavalin A with a-mannans from a variety of microorganisms. J Biol Chem 243: 2003–2007

    PubMed  CAS  Google Scholar 

  • Sternbach H (1991) Chromatographische Methoden in der Biochemie. Thieme, Stuttgart New York

    Google Scholar 

  • Svennerholm L (1958) Quantitative estimation of sialic acids. III. An anion exchange resin method. Acta Chem Scand 12: 547–554

    Article  CAS  Google Scholar 

  • Turner RH, Liener IE (1975) The use of glutaraldehyde-treated erythrocytes for assaying the agglutinating activity. Anal Biochem 68: 651–653

    Article  PubMed  CAS  Google Scholar 

  • van Driessche E, Beeckmans S, Dejaegere R, Kanarek L (1983) A critical study on the purification of potato lectin (Solanum tuberosum L.) In: Bog-Hansen TC, Spengler GA (eds) Lectins-biology, biochemistry, clinical biochemistry Vol 3, p629–638

    Google Scholar 

  • Vang O, Larsen KP, Bøg-Hansen TC (1986) A new quantitative and highly specific assay for lectin binding activity. In: Bøg-Hansen TC, van Driessche E (eds) Lectins—biology, biochemistry, clinical biochemistry Vol 5, p638–644

    Google Scholar 

  • Whitmore FW (1992) A hemagglutinating substance in chitin. BioTechniques 12: 202–208

    PubMed  CAS  Google Scholar 

  • Williams BL, Wilson K (1984) Methoden der Biochemie. Thieme, Stuttgart New York

    Google Scholar 

  • Wilson K, Goulding KH (1986) A biologist’s guide to principles and techniques of practical biochemistry. Edward Arnold, London

    Google Scholar 

  • Young NM, Leon MA (1978) Preparation of affinity chromatography media from soluble polysaccharides by cross linkage with divinyl sulfone. Carbohydr Res 66: 299–302

    Article  CAS  Google Scholar 

Download references

Authors
  1. H. Rüdiger
    View author publications

    Search author on:PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Institut für Physiologische Chemie, Ludwig-Maximilians-Universität, Veterinärstraße 13, D-80539, München, Germany

    Hans-Joachim Gabius  & Sigrun Gabius  & 

Rights and permissions

Reprints and permissions

Copyright information

© 1993 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Rüdiger, H. (1993). Isolation of Plant Lectins. In: Gabius, HJ., Gabius, S. (eds) Lectins and Glycobiology. Springer Laboratory. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-77944-2_4

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-77944-2_4

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-77946-6

  • Online ISBN: 978-3-642-77944-2

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics