Chromatographic properties of denatured skin and bone collagens on hydroxyapatite.
Denatured collagen samples extracted from the skin and bone of lathyritic rats with guanidine hydrochloride were chromatographed on hydroxyapatite columns. A major fraction of the bone extract that was rich in alpha chain showed a stronger binding to hydroxyapatite when compared to the corresponding fraction from skin. Thus, bone collagen shows a special affinity for hydroxyapatite after isolation and denaturation.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D001842:Bone and Bones / Q000032:analysis; D005591:Chemical Fractionation; D002845:Chromatography; D003094:Collagen / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006882:Hydroxyapatites; D007842:Lathyrism / Q000378:metabolism; D051381:Rats; D012867:Skin / Q000032:analysis
D000596:Amino Acids; D006882:Hydroxyapatites; D003094:Collagen