Some observations on the ageing in vitro of reprecipitated collagen fibres.
The changes in solubility and amounts of reducible cross-links have been studied during "ageing" in vitro of reprecipitated rat skin collagen fibres by incubation at 37 degrees C. Fibres from pre-reduced collagen devoid of aldehyde precursors became insoluble at the same rate as that of normal fibres during "ageing". Insolubilization occurred at a much faster rate in the presence of oxygen than in air and was almost completely inhibited when oxygen was excluded. The rate of decline of the reducible cross-links was, however, unaffected by oxygen tension. The results indicate that, during "ageing" in vitro, conversion of the lysine-derived cross-links to a non-reducible form is not associated with solubility changes. The relationship of these in vitro changes to those ocurring in vivo is unknown.
D000818:Animals; D001842:Bone and Bones; D002417:Cattle; D011232:Chemical Precipitation; D003094:Collagen; D004355:Drug Stability; D006901:Hydroxylysine / Q000032:analysis; D007700:Kinetics; D046911:Macromolecular Substances; D009646:Norleucine / Q000032:analysis; D011485:Protein Binding; D051381:Rats; D012867:Skin; D012995:Solubility; D013997:Time Factors
D046911:Macromolecular Substances; D006901:Hydroxylysine; D009646:Norleucine; D003094:Collagen