Imamura T, Kambara T
Department of Allergy, Kumamoto University Medical School, Japan.
Adv Exp Med Biol. 1989;247B:67-72. doi: 10.1007/978-1-4615-9546-5_11.
Kallikrein inhibitor in plasma (KIP) was purified, and the share in the kallikrein inhibitory capacity of guinea pig plasma was estimated by depletion of the inhibitory activity of KIP with anti-KIP IgG. And KIP was characterized the inhibitory activity using various proteases. The purified KIP exhibited a single band on SDS-gel electrophoresis and the molecular weight was 64,000. KIP inhibited plasma kallikrein dose-dependently and time-dependently, forming a complex with kallikrein with the molecular weight of 137,000. Since the kallikrein inhibitory capacity of guinea pig plasma was completely depleted by anti-KIP IgG that inactivated kallikrein inhibitory activity of KIP, KIP was likely to be the major kallikrein inhibitor in guinea pig plasma. KIP inhibited trypsin and elastase, but not chymotrypsin. The Inhibitory spectrum of KIP was different from the spectrum of each protease inhibitor in human plasma, but was similar to the spectrum of contrapsin in mouse plasma. These results indicated that guinea pig plasma had a different mechanism for kallikrein inhibition, compared with human plasma.
纯化了血浆激肽释放酶抑制剂(KIP),并通过用抗KIP IgG耗尽KIP的抑制活性来估计其在豚鼠血浆激肽释放酶抑制能力中所占的份额。并且使用各种蛋白酶对KIP的抑制活性进行了表征。纯化的KIP在SDS凝胶电泳上呈现单一条带,分子量为64,000。KIP对血浆激肽释放酶的抑制呈剂量依赖性和时间依赖性,与激肽释放酶形成分子量为137,000的复合物。由于抗KIP IgG完全耗尽了豚鼠血浆的激肽释放酶抑制能力,该抗体会使KIP的激肽释放酶抑制活性失活,因此KIP可能是豚鼠血浆中主要的激肽释放酶抑制剂。KIP抑制胰蛋白酶和弹性蛋白酶,但不抑制糜蛋白酶。KIP的抑制谱与人类血浆中每种蛋白酶抑制剂的谱不同,但与小鼠血浆中抗胰蛋白酶的谱相似。这些结果表明,与人类血浆相比,豚鼠血浆具有不同的激肽释放酶抑制机制。