The C-terminus of type I collagen is a major binding site for heparin.
The binding of collagens and fragments of type I collagen to heparin was studied by gel electrophoresis and affinity chromatography. Samples bound in 150 mM NaCl/10 mM Hepes (pH 6.5) were eluted with 2 M NaCl, 6 M urea, or a linear gradient of 0.15-1.0 M NaCl. The triple-helical conformation was shown to be essential for binding. The vertebrate collagenase-generated C-terminal fragment, TCB, was shown to have greater binding affinity for heparin than the N-terminal TCA fragment. Both type II collagen and the NC1 domain of type IV collagen bound to heparin, whereas pepsin-solubilized tetrameric type IV failed to bind.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002846:Chromatography, Affinity; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D051379:Mice; D003012:Microbial Collagenase / Q000378:metabolism; D011487:Protein Conformation
D006493:Heparin; D003094:Collagen; D003012:Microbial Collagenase