An acidic glycoprotein (100-K fucose-rich glycoprotein) from calf skin.
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.
D000818:Animals; D000831:Animals, Newborn; D002417:Cattle; D006023:Glycoproteins / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009844:Oligosaccharides / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis; D012794:Sialic Acids / Q000032:analysis; D012867:Skin / Q000032:analysis*; D014357:Trypsin
D006023:Glycoproteins; D009844:Oligosaccharides; D010446:Peptide Fragments; D012794:Sialic Acids; C044839:fucose-rich glycoprotein 100-K; D014357:Trypsin