Characterization of a hydrophilic form of Thy-1 purified from human cerebrospinal fluid.

摘要: Thy-1 is a developmentally regulated cell surface glycoprotein in nervous tissue. An inositol-containing glycolipid structure covalently attached to its carboxyl terminus, which anchors the protein membrane. In present paper we report characterization of water-soluble form Thy-1, purified from human cerebrospinal fluid (CSF). contrast membrane-bound (M-Thy-1) isolated brain cerebral cortex, CSF-Thy-1 behaved like completely hydrophilic glycoprotein, as analyzed by charge-shift electrophoresis presence detergents and liposome incorporation experiments. displayed slightly higher apparent molecular weight sodium dodecyl sulfate-polyacrylamide gel than M-Thy-1. Digestions with endoglycosidases demonstrated that this difference size was correlated different processing three N-linked oligosaccharides, mobilities deglycosylated molecules were indistinguishable sulfate gels. A Pronase-resistant carboxyl-terminal fragment after trypsin digestion compared corresponding M-Thy-1, obtained treatment either bacterial phosphatidylinositol-specific phospholipase C or serum (as source D). The major identically, respect charge, M-Thy-1 solubilized D. These findings suggest an vivo release phosphatidylinositol-anchored cells action endogenous