血浆前激肽释放酶：分离、特性及激活机制
Plasma prekallikrein: isolation, characterization, and mechanism of activation.
作者信息
Wuepper K D, Cochrane C G
出版信息
J Exp Med. 1972 Jan;135(1):1-20. doi: 10.1084/jem.135.1.1.
Abstract
The precursor of the kinin-forming enzyme, prekallikrein, was isolated from rabbit plasma protected from activation during preparatory procedures. Prekallikrein was shown to be a 4.5S gamma(1)-glycoprotein with an isoelectric point of 5.9 and a mol wt of 99,900. The proenzyme was activated at neutral pH by an enzyme from rabbit or human plasma we have termed prekallikrein activator (PKA) or by trypsin. Prekallikrein was activated by PKA by a process of enzymatic scission. This resulted in the appearance of two fragments; the larger of these possessed kallikrein activity.
摘要
激肽形成酶的前体，即前激肽释放酶，是从兔血浆中分离出来的，在制备过程中受到保护未被激活。前激肽释放酶被证明是一种4.5S的γ(1) -糖蛋白，等电点为5.9，分子量为99,900。该酶原在中性pH条件下可被我们称为前激肽释放酶激活剂（PKA）的兔或人血浆中的一种酶激活，也可被胰蛋白酶激活。前激肽释放酶通过酶促裂解过程被PKA激活。这导致出现两个片段；其中较大的片段具有激肽释放酶活性。
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