Reboul A, Prandini M H, Colomb M G
Laboratoire d'Immunochimie-CEN-G, INSERM U238, unité alliée CNRS, USTMG, Grenoble, France.
Biochem J. 1987 May 15;244(1):117-21. doi: 10.1042/bj2440117.
The effects of proteolysis and deglycosylation on C1 inhibitor (C1Inh) were tested with respect to both its ability to form complexes with C1s and its capacity to block C1 autoactivation. Limited proteolysis of C1Inh by Staphylococcus aureus V8 proteinase, proline-specific endopeptidase or elastase generated a major high-Mr (approximately 86,000) fragment. In contrast with the fragment produced by elastase, which was inactive, the fragments resulting from V8 proteinase and proline-specific endopeptidase treatment retained activity. Deglycosylation with N-glycanase or O-glycanase, or both, had no major effect on the functional activity of C1Inh.
就其与C1s形成复合物的能力及其阻断C1自激活的能力而言，测试了蛋白水解和去糖基化对C1抑制剂（C1Inh）的影响。金黄色葡萄球菌V8蛋白酶、脯氨酸特异性内肽酶或弹性蛋白酶对C1Inh进行有限的蛋白水解产生了一个主要的高分子量（约86,000）片段。与弹性蛋白酶产生的无活性片段相反，V8蛋白酶和脯氨酸特异性内肽酶处理产生的片段保留了活性。用N-聚糖酶或O-聚糖酶或两者进行去糖基化对C1Inh的功能活性没有重大影响。
