Taby O, Chabbat J, Steinbuch M
Centre National de Transfusion Sanguine, Les Ulis, France.
Thromb Res. 1990 Jul 1;59(1):27-35. doi: 10.1016/0049-3848(90)90268-h.
The study of the interaction between activated protein C (APC) and non-plasmatic inhibitors allowed us to demonstrate that aprotinin is a potent competitive inhibitor of APC with a Ki of 1.35 mumol/L. It was possible to adsorb immunopurified protein C (PC) activated by venom activator to insolubilized aprotinin and to recover the active enzyme after elution by HCl 0.1 N or by a chaotropic ion, for example KSCN 3 mol/L. The interaction involved the active-site of the enzyme since PC and DIP-APC did not bind to the matrix. Thus, APC could be purified, after activation, in a one-stage procedure out of a mixture of protein such as a prothrombin complex concentrate.
对活化蛋白C（APC）与非血浆抑制剂之间相互作用的研究使我们能够证明，抑肽酶是APC的一种强效竞争性抑制剂，其抑制常数（Ki）为1.35 μmol/L。可以将经蛇毒激活剂激活的免疫纯化蛋白C（PC）吸附到不溶性抑肽酶上，并在通过0.1 N盐酸或离液剂（如3 mol/L硫氰酸钾）洗脱后回收活性酶。这种相互作用涉及酶的活性位点，因为PC和二异丙基磷酰化APC不与基质结合。因此，活化后的APC可以通过一步法从诸如凝血酶原复合物浓缩物等蛋白质混合物中纯化出来。
