Abstract
Two Gramineae species, oat and maize, are compared with wheat and barley to see if they contain lectins which are structurally and functionally similar to the Hordeae lectins. Four distinct criteria were examined: localisation of lectin activity in the seed, ability to agglutinate a defined type of erythrocyte in a reaction reversed by monomers or oligomers of n-acetyl-d-glucosamine, ability to bind to the affinity matrix p-aminobenzyl-1-thio-2-acetamido-2-deoxy-β-d-glucopyranoside-substituted Sepharose, and cross-reactivity with monospecific antisera raised to wheat-germ agglutinin. Results indicate that the very close relationship found between the lectins of wheat, barley and rye cannot be extended to those species of Gramineae outside the tribe Hordeae.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Abbreviations
- WGA:
-
wheat-germ agglutinin
References
Allen, A.K., Neuberger, A., Sharon, N. (1973) The purification, composition and specificity of wheat-germ agglutinin. Biochem. J. 131,155–160
Bouchard, P., Moroux, T., Tixier, R., Privat, J.P., Monsigny, M. (1976) An improved method for purification of wheat germ agglutinin by affinity chromatography. Biochemie 58, 1247–1253
Bowles, D., Lis, H., Sharon, N. (1979) Distribution of lectins in membranes of soybean and peanut plants. Planta 145, 193–198
Bowles, D., Marcus, S. (1981) Characterisation of receptors for the endegenous lectins of soybean and jackbean seeds. FEBS Lett. 129, 135–138
Cunningham, B.A., Hemperly, J.J., Hopp, T.P., Edelman, G.M. (1979) Favin versus concanavalin A: circularly permuted amino acid sequences. Proc. Natl. Acad. Sci. USA 76, 3218–3222
Foriers, A., Wuidmark, C., Sharon, N., Strosberg, A.D. (1977) Extensive sequence homologies among lectins from leguminous plants. Biochem. Biophys. Res. Commun. 75, 980–986
Foriers, A., Neve, R.D., Kanarek, L., Strosberg, A.D. (1978) Common ancestor for concanavalin A and lentil lectin. Proc. Natl. Acad. Sci. USA 75, 1136–1139
Goldstein, I.J., Hayes, C.E. (1978) The lectins: carbohydrate binding proteins of plants and animals. Adv. Carbohydr. Chem. Biochem. 35, 127–340
Hemperly, J.J., Hopp, T.P., Becker, J.W., Cunningham, B.A. (1979) The chemical characterisation of favin, a lectin isolated from Vicia faba. J. Biol. Chem. 254,6803–6810
Lis, H., Sharon, N. (1980) The biochemistry of plants: a comprehensive treatise, vol. 6, Marcus, A., ed. Academic Press, New York London
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951) Protein measurement with the folin-phenol reagent. J. Biol. Chem. 193, 265–275
Miller, R.C., Bowles, D.J. (1982a) Comparison of endogenous lectins and glycosidases in wheat grains. In: Progress in clinical and biological research, vol. 85, pt B, pp. 535–544, Burger, M.M., Weber, R., eds. A.R. Liss, New York
Miller, R.C., Bowles, D.J. (1982b) A comparative study of the localisation of wheat-germ agglutinin and its potential receptors in wheat. Biochem. J. 206, 571–576
Minetti, M., Aducci, P., Teichner, A. (1976) A new agglutination activity from wheat flour inhibited by tryptophan. Biochim. Biophys. Acta 437, 505–517
Mishkind, M., Keegstra, K., Palevitz, B.A. (1980) Distribution of wheat germ agglutinin in young wheat plants. Plant Physiol. 66, 950–955
Mishkind, M., Raskhel, N.V., Palevitz, B.A., Keegstra, K. (1982) Immunocytochemical localisation of wheat germ agglutinin in wheat. J. Cell. Biol. 92, 753–764
Monsigny, M., Sene, C., Obrenovitch, A., Roche, A.C., Delmotte, F., Boschetti, E. (1979) Properties of succinylated wheat germ agglutinin. Eur. J. Biochem. 98, 39–45
Peumans, W.J., Stinissen, H.M., Carlier, A.R. (1982a) Isolation and partial characterisation of wheat-germ-agglutinin-like lectins from rye (Secale cereale) and barley (Hordeum vulgare) embryos. Biochem. J. 203, 239–243
Peumans, W.J., Stinissen, H.M., Carlier, A.R. (1982b) A genetic basis for the origin of six different isolectins in hexaploid wheat. Planta 154, 562–567
Peumans, W.J., Stinissen, H.M., Carlier, A.R. (1982c) Subunit exchange between lectins from different cereal species. Planta 154, 568–572
Rice, R.H., Etzler, M.E. (1975) Chemical modification and hybridisation of wheat germ agglutinin. Biochemistry 14, 4093–4099
Richardson, C., Blumenthal, K.M., Freishei, J.H., Behnke, W.D. (1978) The complete amino acid sequence of the α-subunit of pea lectin, Pisum sativum. Biochim. Biophys. Acta 537, 310–319
Sedmark, J.J., Grossberg, S.E. (1977) A rapid sensitive and versatile assay for protein using Coomassie Brilliant blue G250. Analytical Biochem. 79, 544–552
van Driessche, E., Foriers, A., Strosberg, A.D., Kanarek, L., (1976) N-terminal sequences of the α and β subunits of the lectin from the Garden Pea (Pisum sativum). FEBS Lett. 71, 220–222
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Miller, R.C., Bowles, D.J. Interrelationships between Gramineae lectins. Planta 157, 138–142 (1983). https://doi.org/10.1007/BF00393647
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00393647