Cell surface labeling of proteins and glycoproteins of some human cultured lymphoid cells.
Cell surface proteins and glycoproteins of some human lymphoblastoid- and neoplastic hematopoietic cell lines were labeled by three different techniques: a) lactoperoxidase catalyzed iodination, b) galactose oxidase-tritiated sodium borohydride and c) reductive methylation of free amino groups by tritiated sodium borohydride--a modification of the technique known for the radiolabeling of soluble proteins. Electrophoretic analysis (SDS-PAGE) of labeled surface proteins and glycoproteins resulted in comparable and complementary electrophoretic patterns obtained by these three techniques. Electrophoretic patterns of studied lymphoblastoid cell lines were essentially similar, with an intensively labeled group of glycoproteins (gp44, gp31, gp24). These glycoproteins were markedly reduced on studied neoplastic cell lines. Further differences in several large proteins were observed between lymphoblastoid- and neoplastic cell lines.
D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis*; D006801:Humans; D007938:Leukemia / Q000032:analysis*; D008214:Lymphocytes / Q000032:analysis*; D011506:Proteins / Q000032:analysis*
D006023:Glycoproteins; D011506:Proteins