A New Lectin from Meadow Saffron (Colchicum automnale)
Open Access
- 1 December 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 82 (4), 1036-1039
- https://doi.org/10.1104/pp.82.4.1036
Abstract
A lectin has been isolated from tubers of the meadow saffron (Colchicum autumnale). It is an octameric protein (Mr 100,000) composed of 4A- and 4B-subunits of Mr 15,000 and 10,000, respectively. It is a glycoprotein with 4.4% carbohydrate, the main sugars are (N-acetyl-) glucosamine, mannose, fucose, and xylose. Although the Colchicum autumnale agglutinin (CAA) agglutinates human red blood cells, it has a much higher activity with rabbit erythrocytes. With respect to its carbohydrate-binding specificity CAA behaves rather unusually as it is inhibited by lactose, galactose, N-acetylgalactosamine and related sugars when assayed with human red blood cells but not in assays with rabbit erythrocytes.This publication has 9 references indexed in Scilit:
- Isolation and partial characterization of an N-acetylgalactosamine-specific lectin from winter-aconite (Eranthis hyemalis) root tubersBiochemical Journal, 1985
- Properties of potato lectin and the nature of its glycoprotein linkagesBiochemical Journal, 1978
- The quantitation of glucosamine and galactosamine in glycoproteins after hydrolysis in p‐toluenesulphonic acidFEBS Letters, 1975
- Structure of the O-Glycosidically Linked Carbohydrate Units of FetuinJournal of Biological Chemistry, 1974
- The Biochemistry of Plant Lectins (Phytohemagglutinins)Annual Review of Biochemistry, 1973
- An assessment of methanolysis and other factors used in the analysis of carbohydrate-containing materialsBiochemical Journal, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951