Title : Further characterization of the binding of fibronectin to gelatin reveals the presence of different binding interactions.

Pub. Date : 1993 Jul

PMID : 8323285






4 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 The specific interaction between fibronectin and collagen has permitted the isolation of fibronectin from plasma using gelatin-Sepharose affinity matrices. Sepharose fibronectin 1 Homo sapiens
2 The specific interaction between fibronectin and collagen has permitted the isolation of fibronectin from plasma using gelatin-Sepharose affinity matrices. Sepharose fibronectin 1 Homo sapiens
3 (ii) This tightly bound fibronectin could not be eluted from gelatin-Sepharose matrices with strong denaturing agents, such as 8.0 M urea or 6.0 M guanidium chloride. Sepharose fibronectin 1 Homo sapiens
4 (iv) Two fibronectin-derived fragments, CB52kDa and T55 kDa, selectively bound to fresh gelatin-Sepharose but not to gelatin-Sepharose previously employed to purify fibronectin, suggesting that these fragments recognize only the high affinity binding sites in gelatin. Sepharose fibronectin 1 Homo sapiens