[Isolation and purification of biopolymers using an affinity chromatography method. IX. Preparation, properties and use of affinity adsorbents with immobilized polypeptide fragments of collagen].

Autor: Mitina VKh, Frantsuzova NA, Kliashitskiĭ VA, Krasnopol'skiĭ IuM, Sennikov GA, Svets VI, Orekhovich VN
Jazyk: ruština
Zdroj: Bioorganicheskaia khimiia [Bioorg Khim] 1989 Nov; Vol. 15 (11), pp. 1468-73.
Abstrakt: 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.
Databáze: MEDLINE