Isolation and partial characterization of wheat-germ-agglutinin-like lectins from rye (Secale cereale) and barley (Hordeum vulgare) embryos
- 1 April 1982
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 203 (1) , 239-243
- https://doi.org/10.1042/bj2030239
Abstract
Lectins were isolated from embryos of S. cereale (rye) and H. vulgare (barley) by affinity chromatography on immobilized N-acetylglucosamine. Both lectins are dimeric proteins of 2 identical subunits of MW 18,000. They resemble strongly wheat-germ agglutinin with respect to their chemical, physical, biological and immunological properties. [Plant lectins are widely used as powerful tools in cell-surface and complex-carbohydrate research owing to their unique ability to bind specific sugars or sugar-containing macromolecules.].This publication has 14 references indexed in Scilit:
- Crystallographic elucidation of the saccharide binding mode in wheat germ agglutinin and its biological significanceJournal of Molecular Biology, 1980
- The Lectins: Carbohydrate-Binding Proteins of Plants and AnimalsAdvances in Carbohydrate Chemistry and Biochemistry, 1978
- A barley lectin that binds free amino sugars I. Purification and characterizationBiochimica et Biophysica Acta (BBA) - General Subjects, 1976
- The rye embryo system as an alternative to the wheat system for protein synthesis in vitroBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1976
- Wheat germ agglutinin evidence for a genetic basis of multiple formsBiochimica et Biophysica Acta (BBA) - General Subjects, 1976
- Protein—sugar interactions. Association of β‐(1→4) linked N‐acetyl‐D‐glucosamine oligomer derivatives with wheat germ agglutinin (lectin)FEBS Letters, 1974
- Subunit structure of wheat germ agglutininBiochemical and Biophysical Research Communications, 1974
- Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding.1974
- The purification, composition and specificity of wheat-germ agglutininBiochemical Journal, 1973