Summary
A new acidic glycoprotein was isolated from 4 M-guanidiunium chloride which had been extracted from neutral-salt-insoluble fractions of neonatal calf skin. During the process of purification, the glycoprotein co-migrated with proteodermatan sulphate and its sugar components mainly consisted of fucose, mannose and hexosamine. A broad band obtained by sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis suggested that the molecular weight was 100,000. High-voltage electrophoresis, revealed acidic fragments in its tryptic peptides, while its oligosaccharide chains were shown to have on acidic nature by electrophoresis on a cellulose acetate membrane. These results show that the glycoprotein differs from other glycoproteins (fibronectin, laminin, entactin, nidogen and the 31-K protein of chondrocyte membrane) which have been reported in connective tissues.
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Matsunaga, E., Shinkai, H. An acidic glycoprotein (100-K fucose-rich glycoprotein) from calf skin. Arch Dermatol Res 277, 93–97 (1985). https://doi.org/10.1007/BF00414104
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DOI: https://doi.org/10.1007/BF00414104