Isolation and purification of biopolymers using an affinity chromatography method. IX. Preparation, properties and use of affinity adsorbents with immobilized polypeptide fragments of collagen
Mitina, V.K.; Frantsuzova, N.A.; Kliashitskiĭ, V.A.; Krasnopol'skiĭ, I.M.; Sennikov, G.A.; Svets, V.I.; Orekhovich, V.N.
Bioorganicheskaia Khimiia 15(11): 1468-1473
Synthesis and properties of new affinity adsorbents with immobilized polypeptide fragments of collagen molecule (alpha-chains, beta-components, cyanogen bromide peptides) were described. Adsorbents with alpha-chains and alpha 1CB7-peptide had fibronectin binding capacity 1.5-2.0 times higher than commercial gelatin-Sepharose. Commercial production of highly purified fibronectin from human plasma using affinity chromatography on immobilized individual alpha-chains of collagen was developed.