Affinity of placental decorin for collagen.
Decorin was isolated from 7 M urea extract of bovine placental cotyledons by ion-exchange and hydrophobic chromatography. Decorin and its core protein showed a broad band at about 115 kDa and a single band at 47 kDa, respectively by SDS-PAGE. Anti-decorin core protein antiserum from pig skin was reacted with placental decorin and its core protein in western blotting. The NH2-terminal amino acid sequence of core protein from placental cotyledons was not different from that of core protein from skin and bone. Glycosaminoglycan of decorin was identified as dermatan sulfate by electrophoresis on a cellulose-acetate membrane and chondroitinase digestivity. Decorin bound to collagen in the order for type III, I, and V.
Batbayar
T
T
Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan.
Nomura
Y
Y
Ishii
Y
Y
Shirai
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D003094:Collagen / Q000378:metabolism*; D058575:Decorin; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins; D010920:Placenta / Q000737:chemistry*; D011509:Proteoglycans / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D020539:Sequence Analysis, Protein
D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans; D003094:Collagen