Isolation of an actin-binding fragment of fibronectin.
We have identified a specific actin-binding site in the adhesive glycoprotein fibronectin, isolated from chicken fibroblasts. Affinity chromatography of fragments, released from fibronectin by limited proteolysis with trypsin, chymotrypsin and subtilisin, on actin-Sepharose and other protein-Sepharose columns was used to locate the binding site. A 27 000-mol.wt. subtilisin-digest fragment bound efficiently to actin. The results suggest that the actin-binding site is close to, but not identical with, the reported collagen-binding site.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D002846:Chromatography, Affinity; D002918:Chymotrypsin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005353:Fibronectins / Q000378:metabolism*; D005780:Gelatin / Q000378:metabolism; D010446:Peptide Fragments / Q000302:isolation & purification*; D011485:Protein Binding; D013381:Subtilisins / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D000199:Actins; D005353:Fibronectins; D010446:Peptide Fragments; D005780:Gelatin; D013381:Subtilisins; D002918:Chymotrypsin; D014357:Trypsin