Abstract
Two lectins were purified by affinity chromatography from mature peanut (Arachis hypogaea L.) nodules, and compared with the previously characterised seed lectin of this plant. One of the nodule lectins was similar to the seed lectin in its molecular weight and amino-acid composition and ability to bind derivatives of galactose. However, unlike the seed lectin, this nodule lectin appeared to be a glycoprotein and the two lectins were only partially identical in their reaction with antibodies prepared against the seed lectin. The other nodule lectin also appeared to be a glycoprotein but bound mannose/glucose-like sugar derivatives, and differed from the seed lectin in molecular weight, antigenic properties and amino-acid composition.
Similar content being viewed by others
Abbreviations
- Gal:
-
galactose
- Gle:
-
glucose
- GNL:
-
galactose-binding nodule lectin
- Fru:
-
fructose
- MNL:
-
mannosebinding nodule lectin
- M r :
-
rerative molecular mass
- PBS:
-
phosphate-buffered saline
- PSL:
-
peanut seed lectin
- SDS:
-
sodium dodecyl sulphate
- Sorb:
-
sorbitol
References
Allen, K.A., Desai, N.N., Neuberger, A. (1976) The purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity. Biochem. J. 155, 127–135
Ashwell, G. (1966) The phenol-sulfuric acid reaction for carbohydrates. Methods Enzymol. 3, 93–94
Baumann, C., Rudiger, H., Strosberg, A.D. (1979) A comparison of the two lectins from Vicia cracca. FEBS Lett. 10, 216–218
Bloch, R., Burger, M.M. (1974) A rapid procedure for derivatizing agarose with a variety of carbohydrates: its use for affinity chromatography of lectins. FEBS Lett. 44, 286–289
Borrebaeck, C.A.K. (1984) Detection and characterization of a lectin from non-seed tissue of Phaseolus vulgaris. Planta 161, 223–228
Etzler, M.E. (1986) Distribution and function of plant lectins. In: The lectins, pp. 371–435, Liener, I.E., Sharon, N., Goldstein, I.J., eds. Academic Press, New York
Gabriel, O. (1971) Analytical disc gel electrophoresis. Methods Enzymol. 22, 565–578
Gade, W., Jack, M.A., Dahl, J.B., Schmidt, E.L., Wold, F. (1981) The isolation and characterization of a root lectin from soybean (Glycine max (L), Cultivar Chippewa) J. Biol. Chem. 256, 12905–12910
Glossmann, H., Neville, D.M. (1971) Glycoproteins of cell surfaces. A comparative study of three different cell surfaces of the rat. J. Biol. Chem. 246, 6339–6346
Goldstein, I.J., Poretz, R.D. (1986) Isolation and chemical properties of lectins. In: The lectins, pp. 33–247, Liener, I.E., Sharon, N., Goldstein, I.J., eds. Academic Press, New York
Hankins, C.M., Kindinger, J., Shannon, L.M. (1987) The lectins of Sophora japonica 1. Purification, properties and N-terminal amino acid sequences of two lectins from leaves. Plant Physiol. 83, 825–829
Hapner, K.D., Robbins, J.E. (1979) Isolation and properties of a lectin from sainfoin (Onobrychis viciifolia Scop.). Biochim. Biophys. Acta 580, 186–197
hewitt, E.J. (1966) Sand and water culture methods used in the study of plant nutrition. 2nd edn. Commonwealth Agricultural Bureaux, Farnham Royal, England
Kishinevsky, B.D., Law, I.J., Strijdom, B.W. (1988) Detection of lectins in nodulated peanut and soybean plants. Planta 176, 10–18
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685
Law, I.J., Strijdom, B.W. (1984) Properties of lectins in the root and seed of Lotononis bainesii. Plant Physiol. 74, 773–778
Lei, K.S., Drescher, D.G. (1978) Fluorometric amino-acid analysis with o-phthaldialdehyde. Int. J. Biochem. 9, 457–467
Lotan, R., Skutelsky, E., Danon, D., Sharon, N. (1975) The purification, composition and specificity of the anti-T lectin from peanut (Arachis hypogaea). J. Biol. Chem. 250, 8518–8523
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
Pueppke, S.G. (1979) Distribution of lectins in the Jumbo Virginia and Spanish varieties of the peanut, Arachis hypogaea L. Plant Physiol. 64, 575–580
Pueppke, S.G. (1981) Multiple molecular forms of peanut lectin: Classification of isolectins and isolectin distribution among genotypes of the genus Arachis. Arch. Biochem. Biophys. 212, 254–261
Pueppke, S.G., Freund, T.G., Schultz, B.C., Friedman, H.P. (1981) Interaction of lectins from soybean and peanut with rhizobia that nodulate soybean, peanut or both plants. Can. J. Microbiol. 26, 1489–1497
Uy, R., Wold, F. (1977) 1,4-Butanediol diglycidyl ether coupling of carbohydrates to Sepharose: Affinity adsorbents for lectins and glycosidases. Anal. Biochem. 81, 98–107
Verma, D.P.S., Fortin, M.G., Stanley, J., Mauro, V.P., Paurohit, S., Morrison, N. (1986) Nodulins and nodulin genes of Glycine max. Plant Mol. Biol. 7, 51–61
Vincent, J.M. (1970) A manual for the practical study of rootnodule bacteria. Blackwell Scientific Publications, Oxford
Young, N.M., Williams, R.E., Roy, C., Yaguchi, M. (1982) Structural comparison of the lectin from sainfoin (Onobrychis viciifolia) with concanavalin A and other D-mannosespecific lectins. Can. J. Biochem. 60, 933–941
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Law, I.J., Haylett, T. & Strijdom, B.W. Differences in properties of peanut seed lectin and purified galactose- and mannose-binding lectins from nodules of peanut. Planta 176, 19–27 (1988). https://doi.org/10.1007/BF00392475
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00392475