## Abstract Fibronectin, a plasma protein immunologically identical with a major surface protein of normal fibroblasts, was found to bind to collagen and gelatin. A solid phase enzyme immunoassay was used for the binding tests. Collagen, gelatin or various control proteins were adsorbed to a plasti
Cross-linking of fibronectin to collagenous proteins
β Scribed by Deane F. Mosher
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 432 KB
- Volume
- 58
- Category
- Article
- ISSN
- 0300-8177
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β¦ Synopsis
Attempts were made to cross-link several collagenous proteins to fibronectin with Factor XIIIa (plasma transglutaminase). Cross-linking was demonstrated with type I collagen, type II collagen, type III collagen, type V or AB collagen, and alpha 1(I)-CB7 and alpha 1(I)-CB8 cyanogen bromide fragments of type I collagen. Cross-linking was not demonstrated with type IV collagen, Clq, and cyanogen bromide fragment alpha 1(I)-CB6. The pH optimum for cross-linking of alpha 1(I)-CB7 to fibronectin was 8.5 to 9.6. Cross-linking of alpha 1(I)-CB7 to fibronectin was somewhat enhanced at lower than physiological ionic strength.
π SIMILAR VOLUMES
Soluble fibronectin is found in body fluids and media of cultured adherent cells. Insoluble fibronectin is found in tissue stroma and in extracellular niatrices of cultured cells. Fibronectin is a substrate for factor XIII, (plasma transglutaminase) and can be cross-linked t o collagen and t o the 0