Abstract
The hemagglutinin (lectin) associated with the cell walls of hypocotyls from Vigna radiata was greatly purified. At every stage in the purification the hemagglutinating activity coincided exactly with α-galactosidase activity. This suggests that, similar to the seed lectin of the same plant, both activities might be present in the same molecule which has a molecular weight of about 170,000. When the purification was performed in the absence of d-galactose and 2-mercaptoethanol (method A), the native molecule appeared to dissociate into smaller units exhibiting preferentially either α-galactosidase or lectin properties. This indicates that the subunits in the native molecule might be functionally different. The lectin appears to be bound to the cell wall and can rebind to cell walls without participation of its sugar binding sites.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Allen, A.K., Desai, N.N., Neuberger, A., Greeth, J.M. (1978) Properties of potato lectin and the nature of its glycoprotein linkage. Biochem. J. 171, 665–674
Haaß, D., Frey, R., Kauss, H. (1977) Partial purification of lectins from cell walls. Hoppe-Seyler's Z. Physiol. Chem. 358, 1210–1211
Hankins, C.N., Shannon, L.M. (1978) The physical and enzymatic properties of a phytohemagglutinin from mung beans. J. Biol. Chem. 253, 7791–7797
Hankins, C.N., Kindinger, J.I., Shannon, L.M. (1980a) Legume α-galactosidases which have hemagglutinin properties. Plant Physiol. 65, 618–622
Hankins, C.N., Kindinger, J.I., Shannon, L.M. (1980b) Legume α-galactosidase forms devoid of hemagglutinin activity. Plant Physiol. 66, 375–378
Kauss, H., Glaser, Ch. (1974) Carbohydrate-binding proteins from plant cell walls and their possible involvement in extension growth. FEBS Lett. 45, 304–307
Kauss, H., Bowles, D. (1976) Some properties of carbohydrate-binding proteins (lectins) solubilized from cell walls of Phaseolus aureus. Planta 130, 169–174
Kauss, H. (1981) Lectins and their physiological role in slime molds and in higher plants. In: Encyclopedia of plant physiology. New Series. Plant carbohydrates, vol. II, Tanner, W., Loewus, F., eds. Springer, Berlin Heidelberg New York (in press)
Kivirriko, K.J. (1963) Hydroxyproline containing fractions in normal and cortisone treated chick embryo. Acta Physiol. Scand. 60, suppl. 219
Klis, F.M., Eeltink, H. (1979) Changing arabinosylation pattern of wall bound hydroxyproline in bean cell cultures. Planta 144, 479–484
Kurz, G., Wallenfels, K. (1970) d-Galactose, UV-Test mit Galactose-Dehydrogenase. In: Methoden der enzymatischen Analyse, pp. 1241–1249, Bergmeyer, H.E., ed. Verlag Chemie, Weinheim
Lamport, D.T.A. (1973) The glycopeptide linkages of extensin, O-d-galactosyl serine and O-l-arabinosyl hydroxyproline. In: Biogenesis of plant cell wall polysaccharides. pp. 149–165. Loewus, F.A., ed. Academic Press, London
Martin, R.G. and Ames, B.N. (1961) A method for determining the sedimentation behavior of enzymes: Application to protein mixtures. J. Biol. Chem. 236, 1372–1381
Rüchel, R. (1976) Sequential protein analysis from single identified neurons of Aplysia californica — A microelectrophoretic technique involving polyacrylamide gradient gels and isoelectric focussing. J. Histochem. Cytochem. 24, 773–791
Sedmak, J.J., Grossberg, J.F. (1977) A rapid, sensitive and versatile assay for protein using Coomassie brilliant blue G 250. Anal. Biochem. 79, 544–552
Weber, K., Pringle, J.R., Osborn, M. (1972) Measurement of molecular weights by electrophoresis on SDS-acrylamide gel. Methods Enzymol. 26, 3–25
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Haaß, D., Frey, R., Thiesen, M. et al. Partial purification of a hemagglutinin associated with cell walls from hypocotyls of Vigna radiata . Planta 151, 490–496 (1981). https://doi.org/10.1007/BF00386544
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00386544