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.
CITATION STYLE
Nemerow, G. R., Siaw, M. F., & Cooper, N. R. (1986). Purification of the Epstein-Barr virus/C3d complement receptor of human B lymphocytes: antigenic and functional properties of the purified protein. Journal of Virology, 58(2), 709–712. https://doi.org/10.1128/jvi.58.2.709-712.1986
Mendeley helps you to discover research relevant for your work.