Studies on the interaction between heparin and mouse bone collagenase.
Mouse bone collagenase was found to be tightly bound to a heparin-substituted gel at low ionic strength.  The bond was reversible, however, and the collagenase could be elutted at high ionic strength.  In addition to providing a method for purifying the enzyme with high yield, the results suggest that the strong ionic bond between heparin and collagenase may partially explain the mechanism wherein heparin enhances the activity of mouse bone collagenase.
D000818:Animals; D001842:Bone and Bones / Q000201:enzymology; D002846:Chromatography, Affinity; D006493:Heparin / Q000494:pharmacology*; D051379:Mice; D003012:Microbial Collagenase / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D009994:Osmolar Concentration; D011485:Protein Binding; D012685:Sepharose; D013977:Tibia / Q000201:enzymology
D006493:Heparin; D012685:Sepharose; D003012:Microbial Collagenase