Abstract
The Epstein-Barr virus/C3d receptor (CR2) of human B lymphocytes was purified to homogeneity from Raji cells by immunoaffinity chromatography. The average yield of the 145-kilodalton receptor was 400 pmol (50 micrograms) per 10(10) cells, representing an approximate 75% recovery. The isolated 145-kilodalton protein was antigenically and functionally intact as it reacted with several anti-CR2 monoclonal antibodies and bound purified Epstein-Barr virus and C3d,g. These findings with the purified molecule provide an unequivocal demonstration of the dual receptor functions of this protein.
MeSH Terms
B-Lymphocytes/analysis,immunology
Cell Line
Chromatography, Affinity
Complement C3
Complement C3d
Enzyme-Linked Immunosorbent Assay
Epitopes
Herpesvirus 4, Human/metabolism
Humans
Molecular Weight
Receptors, Complement/immunology,isolation & purification,metabolism
Receptors, Complement 3d
Receptors, Virus/immunology,isolation & purification,metabolism
Chemicals
Complement C3
Epitopes
Receptors, Complement
Receptors, Complement 3d
Receptors, Virus
Complement C3d
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Nemerow G R
Siaw M F
Cooper N R
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18 references, click to expand
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