The lectin binding sites on the membranes of the nuclear envelope, mitochondria and the cell surface of human lymphoblastoid cells.
The membranes of the cell surface, the endoplasmic reticulum, outer and inner mitochondrial leaflet and nuclear envelope were isolated from three human lymphoblastoid cell lines. Membrane components were separated by dodecyl sulfate polyacrylamide gel electrophoresis and the gels incubated with the radioiodinated lectins from lentil, castor bean, scarlet runner bean, gorse seed and Roman snail. After gel slicing and counting, the molecular weights of the lectin binding sites were determined. About 20 glycoproteins were identified as constituents of the plasma membrane, a similar glycoprotein distribution was observed in the endoplasmic reticulum. The outer mitochondrial membrane contained some impurities from the plasma membrane, the inner mitochondrial membrane lacked specific lectin receptors. Two prominent glycoproteins with molecular weights of 70 000 and 60 000 were identified with the castor bean lectin in the nuclear envelope.
D002460:Cell Line; D002462:Cell Membrane / Q000032:analysis*; D004721:Endoplasmic Reticulum / Q000032:analysis; D006801:Humans; D007425:Intracellular Membranes / Q000032:analysis*; D037102:Lectins; D008214:Lymphocytes; D008928:Mitochondria / Q000032:analysis*; D008970:Molecular Weight; D009685:Nuclear Envelope / Q000032:analysis*; D011975:Receptors, Mitogen / Q000032:analysis*
D037102:Lectins; D011975:Receptors, Mitogen