Johansen H T, Briseid K
Adv Exp Med Biol. 1986;198 Pt A:147-53. doi: 10.1007/978-1-4684-5143-6_20.
Plasma kallikrein activated spontaneously during the purification of prekallikrein (I) and acetone-activated plasma kallikrein (II) were at pH 7.4 both capable of reducing the capacity of purified human high molecular weight kininogen (HMrK) to function as cofactor in the contact phase activation of factor XII in a crude plasma preparation. At pH 6.8 only I had such an effect. SDS polyacrylamide gel electrophoresis with reduction indicated that both I and II contained kallikrein as a cleaved 'three-chain molecule. I contained in addition a Mr 49,000 fraction reflecting possibly uncleaved heavy chain. The registration of reduced cofactor function of HMrK induced by plasma kallikrein is discussed in view of the assay procedure used.
在激肽释放酶原（I）纯化过程中自发激活的血浆激肽释放酶以及丙酮激活的血浆激肽释放酶（II），在pH 7.4时均能够降低纯化的人高分子量激肽原（HMrK）在粗血浆制剂中作为因子XII接触相激活辅因子的功能。在pH 6.8时，只有I有这种作用。还原条件下的SDS聚丙烯酰胺凝胶电泳表明，I和II均含有作为裂解的“三链分子”的激肽释放酶。I还含有一个分子量为49,000的组分，可能反映未裂解的重链。鉴于所使用的测定方法，讨论了血浆激肽释放酶诱导的HMrK辅因子功能降低的记录情况。
