Chauvet J, Chabbat J, Acher R
Int J Pept Protein Res. 1986 Jul;28(1):85-90. doi: 10.1111/j.1399-3011.1986.tb03232.x.
The light chain of plasmin, prepared by selective reduction of the interchain disulfide bridges, can be separated from the heavy chain by affinity adsorption onto Kunitz inhibitor/Sepharose. This adsorption involves the active center of plasmin because it does not occur if the light chain is derived from a plasmin previously blocked by the active site titrant p-nitrophenyl-p'-guanidinobenzoate. It can be deduced that the conformation of the inhibitor binding domain of plasmin is preserved in the free light chain.
通过选择性还原链间二硫键制备的纤溶酶轻链，可通过亲和吸附到库尼茨抑制剂/琼脂糖凝胶上与重链分离。这种吸附涉及纤溶酶的活性中心，因为如果轻链来自先前被活性位点滴定剂对硝基苯基 - 对'-胍基苯甲酸酯阻断的纤溶酶，则不会发生这种吸附。可以推断，纤溶酶抑制剂结合结构域的构象在游离轻链中得以保留。
