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血清对蛋白水解酶的抑制作用研究。I. 以I131标记的纤维蛋白为底物研究血清对胰蛋白酶、纤溶酶和糜蛋白酶的抑制机制。

Studies on the inhibition of proteolytic enzymes by serum. I. The mechanism of the inhibition of trypsin, plasmin, and chymotrypsin by serum using fibrin tagged with I131 as a substrate.

作者信息

SHULMAN N R

出版信息

J Exp Med. 1952 Jun;95(6):571-91. doi: 10.1084/jem.95.6.571.

DOI:10.1084/jem.95.6.571

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2212089/

Abstract

The mechanism of the inhibition of trypsin, plasmin, and chymotrypsin by serum was studied using fibrin tagged with radioactive iodine as a substrate. Enzyme-inhibitor relationships were studied by: (a) varying the concentration of serum; (b) varying the concentration of enzyme; and (c) by diluting the enzyme-serum mixture. The results indicate that the inhibition of trypsin, plasmin, and chymotrypsin is a stoichiometric and irreversible reaction. By using the Lineweaver-Burk graphical method of analysis it was demonstrated that the inhibition of trypsin and chymotrypsin is a non-competitive reaction. This finding supports the conclusion that inhibition by serum is an irreversible type of reaction. The substrate was found to exert a retarding effect on the activity of plasmin. The possibility of a plasmin inhibitor in fibrinogen was suggested. The suitability of the various procedures used in evaluating serum proteolytic inhibition was discussed.

摘要

以放射性碘标记的纤维蛋白为底物，研究了血清对胰蛋白酶、纤溶酶和糜蛋白酶的抑制机制。通过以下方式研究酶 - 抑制剂关系：(a) 改变血清浓度；(b) 改变酶浓度；(c) 稀释酶 - 血清混合物。结果表明，血清对胰蛋白酶、纤溶酶和糜蛋白酶的抑制是一种化学计量且不可逆的反应。通过使用Lineweaver - Burk图解分析法表明，血清对胰蛋白酶和糜蛋白酶的抑制是非竞争性反应。这一发现支持了血清抑制是一种不可逆反应类型的结论。发现底物对纤溶酶的活性有抑制作用。提示纤维蛋白原中可能存在纤溶酶抑制剂。讨论了用于评估血清蛋白水解抑制作用的各种方法的适用性。