通过蛋白水解作用由变性马血浆形成的耐酸蛋白酶抑制多肽。

Acid-stable protease inhibiting polypeptides formed from denatured horse plasma by proteolysis.

Pellegrini A, Hägeli G, von Fellenberg R

Department of Veterinary Physiology, University of Zürich, Switzerland.

Comp Biochem Physiol B. 1987;88(1):237-42. doi: 10.1016/0305-0491(87)90107-6.

Abstract

Trypsin digestion of perchloric acid precipitated horse plasma yielded polypeptides with inhibitory properties for trypsin, chymotrypsin and, to a small extent, kallikrein. 2. The Mr of the inhibitory polypeptides were 73,000 and 24,000. 3. The number, enzyme specificity and Mr of the inhibitory polypeptides differed from the values known for the human being. 4. The inhibitory polypeptides were purified by affinity chromatography on Sepharose-trypsin and by gel filtration through Sephadex G-75. 5. Protease inhibitory polypeptides were generated in the same manner by chymotrypsin, elastase, proteinase K, pronase, collagenase, papain and subtilisin. 6. The number and electrophoretic migration of the inhibitory polypeptides obtained with the different enzymes were variable. 7. The enzyme specificity was constant since all polypeptides inhibited only trypsin, chymotrypsin and kallikrein to a small extent. 8. None of the inhibitory polypeptides were immunologically related to native plasma proteins or plasma protease inhibitors.

摘要

用胰蛋白酶消化高氯酸沉淀的马血浆，产生了对胰蛋白酶、胰凝乳蛋白酶以及在较小程度上对激肽释放酶具有抑制特性的多肽。2. 这些抑制性多肽的相对分子质量分别为73,000和24,000。3. 抑制性多肽的数量、酶特异性和相对分子质量与人类已知的值不同。4. 通过在琼脂糖-胰蛋白酶上进行亲和层析以及通过葡聚糖凝胶G-75进行凝胶过滤来纯化抑制性多肽。5. 胰凝乳蛋白酶、弹性蛋白酶、蛋白酶K、链霉蛋白酶、胶原酶、木瓜蛋白酶和枯草杆菌蛋白酶以相同方式产生蛋白酶抑制性多肽。6. 用不同酶获得的抑制性多肽的数量和电泳迁移率是可变的。7. 酶特异性是恒定的，因为所有多肽仅对胰蛋白酶、胰凝乳蛋白酶和激肽释放酶有较小程度的抑制作用。8. 没有一种抑制性多肽与天然血浆蛋白或血浆蛋白酶抑制剂存在免疫相关性。