Sakamoto S, Sakamoto M, Goldhaber P, Glimcher M J
Biochim Biophys Acta. 1975 Mar 14;385(1):41-50. doi: 10.1016/0304-4165(75)90072-0.
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.
研究发现,小鼠骨胶原酶在低离子强度下与肝素替代凝胶紧密结合。然而,这种结合是可逆的,胶原酶可在高离子强度下洗脱。这些结果除了提供一种高产率纯化该酶的方法外,还表明肝素与胶原酶之间的强离子键可能部分解释了肝素增强小鼠骨胶原酶活性的机制。