Synthesis of collagen by chick calvaria in the presence of 2,2'-bipyridyl. Lack of the aminoterminal extension peptides.
A precursor of type I collagen was accumulated when cranial bones from embryonic chicken were cultured in vitro in the presence of 2,2'-bipyridyl. While biochemical studies demonstrate that the precursor was present as a covalently linked trimer, evaluation of electron micrographs of segment-long-spacing aggregates show that the molecules of this precursor have an extension at the carboxy terminus only. These data provide further evidence that the inter-chain disulfide bonds in procollagen are located at the carboxy-terminal extension, and secondly, that 2,2'-bipyridyl does not interfere with a normal cleavage of procollagen peptides at the amino terminus, but inhibits the cleavage of the carboxy-terminal procollagen peptides.
D015082:2,2'-Dipyridyl / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D003094:Collagen / Q000096:biosynthesis* / Q000302:isolation & purification; D004220:Disulfides; D010455:Peptides; D011347:Procollagen / Q000096:biosynthesis / Q000302:isolation & purification; D011725:Pyridines / Q000378:metabolism*; D012886:Skull / Q000032:analysis*
D004220:Disulfides; D010455:Peptides; D011347:Procollagen; D011725:Pyridines; D015082:2,2'-Dipyridyl; D003094:Collagen