Abstract: Two high purity glycoprotein components each having a molecular weight of about 65,000 daltons and having activity as trypsin inhibitors and inhibitors of endothelial cell growth are obtained from bovine cartilage extract. A guanidine hydrochloride extract of bovine cartilage is subjected to ammonium sulfate salt fractionation, DEAE-Sephadex ion exchange chromatography, SP-Sephadex ion exchange chromatography and Con A-Sepharose affinity chromatography to isolate these glycoproteins in a high purity preparation.

Abstract: A serum albumin fraction is prepared in high yield and purity from plasma and other albumin-containing blood protein fractions by contacting with a resinous polymeric material having a high capacity for adsorption of albumin, heating at 65.degree. C-72.degree. C for about 1-4 hours while maintaining a pH of 5.0-5.5, and then selectively eluting the albumin from the resin-protein mixture at a pH of 3.5-4.5. The resinous polymeric materials are water-insoluble, cross-linked polyelectrolyte copolymers of ethylene and maleic anhydride containing pendant dimethylaminopropyl functional groups.

Abstract: A serum albumin fraction is prepared in high yield and purity from plasma and other albumin-containing blood protein fractions by contacting with a resinous polymeric material having a high capacity for adsorption of albumin, heating at 65.degree.-72.degree. C for about 1-4 hours while maintaining a pH of 5.0-5.5, and then selectively eluting the albumin from the resin-protein mixture at a pH of 3.5-4.5. The resinous polymeric materials are diloweralkylaminoloweralkyl-substituted cross-linked dextran polymers.