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Title: Immunochemical characterization of a 150 000 dalton human fibroblast surface glycoprotein
Authors: Verlinden, J
Van Leuven, Freddy
Cassiman, Jean-Jacques
Van den Berghe, Herman #
Issue Date: Jun-1981
Series Title: Biochimica et Biophysica Acta vol:667 issue:1 pages:1-14
Abstract: The characterization of a human fibroblast surface glycoprotein, visualized by crossed immunoelectrophoresis using rabbit antibodies against whole fibroblasts, is described. The antigen is synthesized by fibroblasts in culture and was localized both intracellularly and at the cell surface. It was highly antigenic and was detected only in human cells of mesenchymal origin. The glycoprotein occurred in two different forms with alpha 2 and beta electrophoretic mobility. The slow migrating amphiphilic beta form was localized at the cell surface and showed a single protein band with an apparent molecular weight of 150 000 in SDS-polyacrylamide gel electrophoresis. By external papain treatment of intact viable cells, a water-soluble molecule was released with a reduced molecular weight (140 000) and an increased electrophoretic mobility as compared to the native membrane component. This hydrophilic form was also present intracellularly in fibroblasts not treated with exogeneous proteases. The observation that the detergent-solubilized beta form was irreversibly converted to a more anodic form by incubation of whole cell extract at acidic pH, suggested that the intracellular protein represented a lysosomal degradation product of native internalized fibroblast surface glycoprotein.
ISSN: 0006-3002
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Associated Laboratories - miscellaneous (-)
Human Mutations and Polymorphisms Section (-)
Clinical Genetics Section (-)
Forensic Biomedical Sciences
Department of Human Genetics - miscellaneous
# (joint) last author

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