{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:44:28Z","timestamp":1786977868877,"version":"build-2736575974"},"reference-count":32,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2009,7,27]],"date-time":"2009-07-27T00:00:00Z","timestamp":1248652800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Biomed Mater Res"],"published-print":{"date-parts":[[2010,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>A porous keratin scaffold, prepared from the reduced keratin solution, has shown good cell viability which makes it a potential candidate for cell seeding. An aqueous solution of reduced keratin was extracted from horn meal using a mixture of urea, sodium dodecyl sulfate, mercaptoethanol, and water at 60\u00b0C. The molecular mass of the extracted keratin is found to be ranging between 225 and 150 KDa. The CD spectrum of aqueous solution of keratin shows the presence of \u221e\u2010helical structure with \u03b2\u2010turns as negative absorption band at 225 nm and as positive absorption band at 195 nm. The FTIR spectrum of the same confirms \u221e\u2010helical structure with \u03b2\u2010turns. Its characteristic absorption bands are assigned mainly to the peptide bonds for amide I, II, and III respectively. DSC and TGA data of the reduced keratin peaks fall in region 200\u00b0C\u2013250\u00b0C and 200\u00b0C\u2013400\u00b0C temperatures, respectively. They correspond to the \u221e\u2010helix denaturation of the material. \u00a9 2009 Wiley Periodicals, Inc. 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