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- W2000834031 abstract "Summary Affinity chromatography on a concanavalin A–Sepharose support was used to isolate two glycoprotein fractions from a heat- and acid-stable fraction of ovine milk. One of these glycoprotein fractions was purified by rechromatography on DEAE-cellulose to essentially a pure protein yielding a single band on gel electro-phoresis. The apparent M r of this glycoprotein (GP2) as estimated by electrophoresis was 50500. It contained 8·88% carbohydrate and 0·61% P. The other glycoprotein fraction (GP3) contained 0·53% P and 17·76% carbohydrate including sialic acid, mannose, galactose, fucose, galactosamine and glucosamine. It appeared on electrophoresis in acrylamide gels as a slow-moving broad band. On similar treatment in the presence of sodium dodecyl sulphate it revealed four glycoprotein zones with apparent M r of 15200, 18300, 23500 and 25300. Both GP2 and GP3 contained low amounts of aromatic and sulphur-containing amino acid residues and large amounts of Asp, Glu, Ser and Leu. GP3 is similar in some respects to the bovine milk heat- and acid-stable fraction constituent, component 3." @default.
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- W2000834031 date "1990-11-01" @default.
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- W2000834031 title "Glycoproteins in the heat- and acid-stable fraction of ovine milk" @default.
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- W2000834031 doi "https://doi.org/10.1017/s0022029900029551" @default.
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