Lectin−Erythrocyte Interaction with External Transmembrane Glycophorin Saccharides Controlling Membrane Internal Cytoskeleta
Author:
Affiliation:
1. Department of Molecular and Cell Pharmacology, University of Wisconsin, Madison, Wisconsin 53706, and Department of Biochemistry, University of Minnesota, 1479 Gortner Avenue, St. Paul, Minnesota 55108
Publisher
American Chemical Society (ACS)
Subject
General Agricultural and Biological Sciences,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jf020261n
Reference13 articles.
1. Anderson, R. A. Glycophorin-protein 4.1: A transmembrane protein complex regulating the erythrocyte membrane skeleton. InMembrane Skeletons and Cytoskeletal Membrane Associations; Bennett, V., Cohen, C. M., Ux, S. L., Palek, J., Eds.; Liss: New York, 1986; pp 223−241.
2. Furthmayr, H.; Glycophorin A: A model membrane protein. InBiology of Complex Carbohydrates; Ginsburg, V., Roggins, P., Eds.; Wiley: New York, 1981; pp 123−197.
3. Stoichiometry of wheat germ agglutinin as a morphology controlling agent and as a morphology controlling agent and as a morphology protective agent for the human erythrocyte.
4. The Thiobarbituric Acid Assay of Sialic Acids
5. An improved method for purification of wheat germ agglutinin (lectin) by affinity chromatography
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