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.