Biosynthesis of a disulphide-bonded short-chain collagen by calf growth-plate cartilage.
Collagen biosynthesis by organ cultures of the hypertrophic zone of calf growth-plate cartilage was studied. It was found that this tissue devotes a large portion of its biosynthetic commitment towards production of a collagen molecule comprising short collagen chains. This collagen is similar to short-chain collagens synthesized by chick-embryo tibiotarsus, rabbit growth-plate cartilage and chick chondrocytes grown in three-dimensional gels. However, in contrast with the collagen synthesized in these three systems, the short-chain collagen synthesized by calf growth-plate hypertrophic cartilage is stabilized by disulphide bonds localized within the pepsin-resistant triple-helical collagenous domains of these molecules.
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000096:biosynthesis*; D004220:Disulfides / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006132:Growth Plate / Q000378:metabolism*; D003012:Microbial Collagenase; D008956:Models, Chemical; D009924:Organ Culture Techniques; D010084:Oxidation-Reduction; D010434:Pepsin A
D004220:Disulfides; D003094:Collagen; D010434:Pepsin A; D003012:Microbial Collagenase