Phaseolus vulgaris isolectin binding to human erythrocytes.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference32 articles.
1. Lectins: Cell-Agglutinating and Sugar-Specific Proteins
2. Looking at Lectins: Do They Function in Recognition Processes?
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4. The Nature of the Cell Surface Receptor Site for Lens culinaris Phytohemagglutinin
5. PURIFICATION AND PROPERTIES OF THE PHYTOHEMAGGLUTININ OF PHASEOLUS VULGARIS
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1. The High Specificities of Phaseolus vulgaris Erythro- and Leukoagglutinating Lectins for Bisecting GlcNAc or β1–6-Linked Branch Structures, Respectively, Are Attributable to Loop B;Journal of Biological Chemistry;2002-05
2. The Role of Valence on the High-Affinity Binding of Griffonia simplicifolia Isolectins to Type A Human Erythrocytes;Biochemistry;1998-11-05
3. Activation and enhanced contact of human T-lymphocytes with autologous red blood cells are required for their stable adherence at 37°;Virchows Archiv B Cell Pathology Including Molecular Pathology;1993-12
4. Aprotinin can inhibit the proteolytic activity of thrombin. A fluorescence and an enzymatic study;European Journal of Biochemistry;1992-07
5. Evaluation of glycoconjugates on the K562 cell surface by means of lectin binding — comparison with human erythrocytes;Glycoconjugate Journal;1984-03
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