Purification of the Epstein-Barr virus/C3d complement receptor of human B lymphocytes: antigenic and functional properties of the purified protein.
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.
G R
GR
Nemerow
M F
MF
Siaw
N R
NR
Cooper
D001402:B-Lymphocytes / Q000032:analysis* / Q000276:immunology; D002460:Cell Line; D002846:Chromatography, Affinity; D003176:Complement C3; D015933:Complement C3d; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D004854:Herpesvirus 4, Human / Q000378:metabolism*; D006801:Humans; D008970:Molecular Weight; D011951:Receptors, Complement / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D017464:Receptors, Complement 3d; D011991:Receptors, Virus / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism
D003176:Complement C3; D000939:Epitopes; D011951:Receptors, Complement; D017464:Receptors, Complement 3d; D011991:Receptors, Virus; D015933:Complement C3d