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• W2065326377 abstract "We have identified and purified a polypeptide region containing the collagen-binding site of the adhesive glycoprotein fibronectin. Chicken cellular fibronectin isolated from cultured embryonic fibroblasts was permitted to bind to gelatin coupled to agarose beads and was then digested extensively with chymotrypsin. A prominent 40,000-dalton fragment of fibronectin consisting of a single polypeptide chain was detected by sodium dodecyl sulfate/polyacrylamide gel electrophoresis of material remaining bound to the gelatin-agarose. This fragment appeared within 10 min after the digestion was initiated and persisted for more than 20 hr. This proteolytic fragment was isolated in electrophoretically pure form and retained its affinity for collagen. Plasma fibronectins from chicken and human blood also contained collagen-binding proteolytic fragments of similar size. This finding suggest that the collagen-binding sites of cellular and plasma fibronectins are homologous." @default.
• W2065326377 created "2016-06-24" @default.
• W2065326377 creator A5026353280 @default.
• W2065326377 creator A5070377346 @default.
• W2065326377 date "1979-03-01" @default.
• W2065326377 modified "2023-10-09" @default.
• W2065326377 title "Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin." @default.
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• W2065326377 doi "https://doi.org/10.1073/pnas.76.3.1160" @default.
• W2065326377 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/383209" @default.
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