Abstract
Glycoprotein material was isolated from bovine aorta by saline extraction and fractionally precipitated with (NH4)2SO4. The glycoprotein material which precipitated between 60–100% saturation of the salt was fractionated by electrophoresis in polyacrylamide gel. The glycoprotein with the fastest mobility was isolated from the gel after repeated electrophoresis as a homogeneous fraction. The glycoprotein contains 17.4 residues of galactose, 3.0 of glucose, 2.9 of fucose, 12.4 of hexosamine and 6.1 of sialic acid per mole of glycoprotein. Sialic acid was selectively removed from the glycoprotein by hydrolysis with neuraminidase, and step-wise hydrolysis of the glycoprotein with β-galactosidase, β-N-acetylglucosaminidase and β-glucosidase revealed certain sequences of mono-saccharides which included galactosyl-N-acetyl-glucosamine and fucosyl-glucosyl-galactose in the glycoprotein.
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