Protein disulphide-isomerase activity in chick-embryo tissues. Correlation with the biosynthesis of procollagen.
Protein disulphide-isomerase activity was determined in homogenates of chick-embryo tissues. Activities were highest in tissues active in procollagen synthesis and were maximal at the developmental stage of maximal procollagen synthesis. These variations in protein disulphide-isomerase activity correlate closely with those previously observed for protocollagen hydroxylase activities.
D000818:Animals; D001842:Bone and Bones / Q000201:enzymology; D002356:Cartilage / Q000201:enzymology; D002642:Chick Embryo; D004220:Disulfides / Q000378:metabolism; D007535:Isomerases / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism; D011347:Procollagen / Q000096:biosynthesis*; D019704:Protein Disulfide-Isomerases; D013710:Tendons / Q000201:enzymology; D014018:Tissue Distribution
D004220:Disulfides; D011347:Procollagen; D006899:Mixed Function Oxygenases; D007535:Isomerases; D019704:Protein Disulfide-Isomerases