胰凝乳蛋白酶原D，一种来自猪胰腺的具有前弹性蛋白酶活性的新型酶原。

Chymotrypsinogen D, a new zymogen from porcine pancreas with proelastolytic activity.

作者信息

Lamy F, Gibson D, Ledoux M, Moreux J C

出版信息

Adv Exp Med Biol. 1977;79:165-75. doi: 10.1007/978-1-4684-9093-0_15.

Abstract

During the purification of propancreatopeptidase E, a proATEEase activity is always copurified. The proelastolytic and proesterolytic activities can be separated on a hydroxylapatite column. The zymogen with potential ATEEase activity has a basic isoelectric point, can be activated by trypsin, and can hydrolyse elastin and ATEE but not ATAME. Its molecular weight is about 26,500 and the NH2-terminal sequence indicates clearly that it belongs to the chymotrypsinogen family, but that it is not chymotrypsinogen A, B, or C. We call it chymotrypsinogen D. Although both pancreatopeptidase E and chymotrypsin D can hydrolyse elastin, the synthetic substrate ATAME is attacked only by pancreatopeptidase E. Therefore, the peptide bonds in elastin cleaved by these two enzymes should be different.

摘要

在胰蛋白酶原E的纯化过程中，一种前弹性蛋白酶活性总是与之一同被纯化。前弹性水解和前酯水解活性可在羟基磷灰石柱上分离。具有潜在弹性蛋白酶活性的酶原具有碱性等电点，可被胰蛋白酶激活，能水解弹性蛋白和弹性蛋白酶底物（ATEE），但不能水解对甲苯磺酰-L-精氨酸甲酯（ATAME）。其分子量约为26500，氨基末端序列清楚地表明它属于胰凝乳蛋白酶原家族，但它不是胰凝乳蛋白酶原A、B或C。我们将其称为胰凝乳蛋白酶原D。尽管胰蛋白酶E和胰凝乳蛋白酶D都能水解弹性蛋白，但合成底物ATAME仅被胰蛋白酶E作用。因此，这两种酶切割弹性蛋白中的肽键应该是不同的。