血浆酸稳定型胰蛋白酶抑制剂的纯化及氨基酸分析

Purification and amino acid analysis of plasma acid stable trypsin inhibitor.

作者信息

Maruyama M, Yamamoto T, Sumi H, Tsushima H, Mihara H, Minamino N

出版信息

Enzyme. 1986;35(4):225-31. doi: 10.1159/000469346.

Abstract

Acid stable trypsin inhibitor (ASTI), with a molecular weight of about 85,000 by gel filtration, specific activity of 1,498 U/mg protein and pI of 1.6, from renal failure patient plasma was first purified. The amino acid composition of the purified ASTI was found to be that of a Gly- and Glu-rich protein which lacked His, closely resembling that of urinary trypsin inhibitor. The NH2-terminal amino acid sequence was Ala-Val-Leu-Pro-Gln-Glu- Glu-Glu-Gly-X-Gly-Gly-Gly-Gln-Leu-Val-Thr-Glu-Val-Thr-Lys-Lys-Glu- Asp-Ser-Ser-Gln-Leu-Gly-Tyr-Ser-Ala-Gly-Pro.

摘要

首先从肾衰竭患者血浆中纯化出了酸稳定胰蛋白酶抑制剂（ASTI），通过凝胶过滤法测得其分子量约为85,000，比活性为1,498 U/mg蛋白质，等电点为1.6。纯化后的ASTI的氨基酸组成被发现是一种富含甘氨酸和谷氨酸的蛋白质，缺乏组氨酸，与尿胰蛋白酶抑制剂非常相似。其氨基末端氨基酸序列为Ala-Val-Leu-Pro-Gln-Glu-Glu-Glu-Gly-X-Gly-Gly-Gly-Gln-Leu-Val-Thr-Glu-Val-Thr-Lys-Lys-Glu-Asp-Ser-Ser-Gln-Leu-Gly-Tyr-Ser-Ala-Gly-Pro。