Influence of glycosylation on allelic and cell-specific Mr variation, receptor processing, and ligand binding of the human complement C3b/C4b receptor

• Published in: The Journal of biological chemistry Vol. 261; no. 13; pp. 5736 - 5744
• Main Authors: Lublin, D M, Griffith, R C, Atkinson, J P
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 05.05.1986; American Society for Biochemistry and Molecular Biology
• Subjects: Alleles; Biological and medical sciences; Cell Line; Complement; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Genetic Variation; Glycoproteins - genetics; Glycoproteins - metabolism; Glycosides; Humans; Kinetics; Leukemia, Myeloid; Ligands; Lymphocytes - metabolism; Molecular immunology; Molecular Weight; Oligosaccharides - analysis; Phenotype; Protein Processing, Post-Translational; Receptors, Complement - genetics; Receptors, Complement - metabolism; Receptors, Complement 3b; Human; Molecular structure; Variations; Complement; Glycosylation; Polymorphism; Biological receptor

The human complement C3b/C4b receptor (CR1), a single chain membrane glycoprotein of Mr approximately 200,000, has several cell-specific Mr variations as well as an allelic variation involving four phenotypes whose Mr values span a range of 90,000. We investigated the role of glycosylation in these...