Reconstituted collagen fibrils. Fibrillar and molecular stability of the collagen upon maturation in vitro.
During the maturation in vitro of reconstituted collagen fibrils prepared from rat skin, the mechanical and thermal stability of collagen increased and the pepsin-solubility decreased. At the same time a larger fraction of the pepsin-soluble collagen attained a lower molecular thermal stability that resulted in a biphasic thermal transition of the soluble collagen. Type-I collagen, with a similar biphasic thermal transition, was isolated from acid-insoluble rat skin collagen.
D000818:Animals; D003094:Collagen / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008297:Male; D010434:Pepsin A; D011489:Protein Denaturation; D051381:Rats; D011919:Rats, Inbred Strains; D012867:Skin / Q000378:metabolism*; D013696:Temperature
D046911:Macromolecular Substances; D003094:Collagen; D010434:Pepsin A