A chromatographic study of the relative affinities of rat bone and skin collagen alpha1 chains for hydroxyapatite.
The affinity of a bone collagen alpha1 chain for hydroxyapatite has been compared to a similarly isolated skin component from the same animals. The chain from bone exhibits a higher affinity for the mineral. This enhanced affinity appears to be related to its primary structure, specifically its hydroxylysine moieties.
D000367:Age Factors; D000629:Aminopropionitrile; D000818:Animals; D001842:Bone and Bones / Q000378:metabolism*; D002845:Chromatography; D003094:Collagen / Q000378:metabolism*; D006882:Hydroxyapatites / Q000378:metabolism*; D006901:Hydroxylysine / Q000378:metabolism; D007842:Lathyrism / Q000139:chemically induced / Q000378:metabolism; D008297:Male; D008722:Methods; D051381:Rats; D012867:Skin / Q000378:metabolism*; D013329:Structure-Activity Relationship
D006882:Hydroxyapatites; D000629:Aminopropionitrile; D006901:Hydroxylysine; D003094:Collagen