Use of biospecific interactions of collagen, fibronectin and their fragments in affinity chromatography
| Autor: | N. A. Frantsuzova, V. I. Shvets, Yu.M. Krasnopolsky, B.A. Klyashchitsky, V. Kh. Mitina |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
Binding Sites Chromatography biology Molecular mass Peptide General Chemistry Cleavage (embryo) Chromatography Affinity Peptide Fragments Fibronectins Fibronectin Sepharose chemistry.chemical_compound chemistry Biochemistry Affinity chromatography biology.protein Humans Spectrophotometry Ultraviolet Cyanogen bromide Collagen Binding site |
| Zdroj: | Journal of Chromatography B: Biomedical Sciences and Applications. 577:267-273 |
| ISSN: | 0378-4347 |
| Popis: | Various aspects of the application of fibronectin-collagen biospecific interactions in affinity chromatography are described. A new biospecific method for one-stage isolation of collagen peptides containing fibronectin-binding sites is proposed. The alpha 1 CB7-peptide of type-I collagen cyanogen bromide cleavage was isolated by means of affinity chromatography on adsorbents containing an immobilized gelatin-binding domain (45,000 relative molecular mass) of fibronectin. The method gives highly purified preparations of alpha 1 CB7-peptide. This peptide, as well as some other collagen molecular fragments (alpha-chains, beta-components, alpha 1 CB8-peptide), were immobilized on Sepharose, and the properties of such affinity adsorbents obtained were studied. Adsorbents with immobilized alpha-chains and alpha 1 CB7-peptide had a fibronectin-binding capacity 1.5-2.0 times higher than commercial gelatin-Sepharose. Large-scale production of highly purified fibronectin from human plasma, using affinity chromatography on immobilized individual alpha-chains of collagen, was developed. |
| Databáze: | OpenAIRE |
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