Modification of biological activities of Ricinus communis agglutinin by cross-linking with formaldehyde
- 1 April 1984
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry and Cell Biology
- Vol. 62 (4) , 203-208
- https://doi.org/10.1139/o84-029
Abstract
Formaldehyde treatment of Ricinus communis agglutinin, a nonmitogenic toxic 120 000 molecular weight (MW) lectin, yielded two distinct protein fractions: one was heterogeneous and contained high molecular weight lectin polymers (> 120 000), and the other was a homogeneous 120 000 MW protein. Both fractions lost their cytotoxicity after formaldehyde treatment and stimulated thymidine incorporation into lymphocytes. Binding of both treated lectin fractions to lymphocytes exhibited positive cooperativity, whereas binding of untreated lectin did not.This publication has 17 references indexed in Scilit:
- Changes in the sensitivity of chick fibroblasts to Ricinus lectin (RCA I) toxicity in relation to the stage of embryo developmentBiochemical Journal, 1979
- The role of concanavalin A dissociation on positive cooperativity of binding with native and fixed erythrocytes.Journal of Biological Chemistry, 1979
- Interaction between the Ricinus sanguineus agglutinin and receptor sites isolated from normal human lymphocytesBiochimie, 1979
- Homology between ricin and Ricinus communie agglutinin: Amino terminal sequence analysis and protein synthesis inhibition studiesArchives of Biochemistry and Biophysics, 1978
- Cooperativity of lectin binding to lymphocytes, and its relevance to mitogenic stimulationBiochimica et Biophysica Acta (BBA) - Biomembranes, 1978
- Cross-Linking of T Cell Mitogens: Effects on B and T Cell Proliferation and Immunoglobulin SynthesisThe Journal of Immunology, 1977
- Structure and toxicity of pure ricinus agglutininBiochimica et Biophysica Acta (BBA) - General Subjects, 1976
- Opposing effects of mitogenic and nonmitogenic lectins on lymphocyte activation. Evidence that wheat germ agglutinin produces a negative signal.Journal of Biological Chemistry, 1976
- Mechanism of human lymphocyte stimulation by concanavalin A: role of valence and surface binding sites.Proceedings of the National Academy of Sciences, 1976
- Cooperative Binding of Concanavalin A to Thymocytes at 4oC and Micro-redistribution of Concanavalin A ReceptorsEuropean Journal of Biochemistry, 1976