PROTEASE INHIBITORS AND THEIR RELATION TO PROTEASE ACTIVITY IN HUMAN-MILK
PROTEASE INHIBITORS AND THEIR RELATION TO PROTEASE ACTIVITY IN HUMAN-MILK
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DOI：
10.1203/00006450-198206000-00016
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发表时间：
1982-01-01
影响因子：
3.6
通讯作者：
WESTROM, B
中科院分区：
文献类型：
--
作者：
LINDBERG, T;OHLSSON, K;WESTROM, B
对 94 名母亲产后第 1 天至 160 天的 190 个牛奶样本中的蛋白酶抑制剂和蛋白酶（酪蛋白分解、弹性蛋白分解和酯分解）活性进行了分析。人乳中的主要蛋白酶抑制剂是α1-抗胰凝乳蛋白酶和α1-抗胰蛋白酶。通过电免疫测定法测量，第1天初乳中的α1-抗胰凝乳蛋白酶水平高于正常血清中的水平。可以证明痕量的间α-胰蛋白酶抑制剂、α2-抗纤溶酶、α2-巨球蛋白、抗凝血酶III或抗白细胞蛋白酶。根据其蛋白酶抑制活性，第 1-3 天的 53 个牛奶样品可分为 2 组。存在蛋白酶抑制活性（n = 35）。 α1-抗胰蛋白酶和α1-抗胰凝乳蛋白酶均显得完整，并且能够与添加的胰蛋白酶或胰凝乳蛋白酶形成复合物，尽管α1-抗胰凝乳蛋白酶的主要部分显示出延迟的电泳迁移率。这些样品中的蛋白水解活性不可检测或很低。尽管存在免疫反应抑制剂，但没有蛋白酶抑制活性 (n = 18)。 α1-抗胰蛋白酶具有与组1类似的沉淀模式，而α1-抗胰蛋白酶的主要部分具有稍微延迟的迁移率以及在α1和β-区域中的2个次要峰。添加与仅存在非反应性抑制剂相容的人胰蛋白酶或胰凝乳蛋白酶后，这些沉淀模式没有改变。这些样品具有酪蛋白分解和酯分解活性，并且在β-区域具有电泳迁移率。第 4 天及之后的所有样品均具有明显的蛋白酶抑制活性。
Protease inhibitors and protease (caseinolytic, elastinolytic and esterolytic) activity were analyzed in 190 milk samples from 94 mothers from day 1 to day 160 after delivery. The main protease inhibitors in human milk are .alpha.1-antichymotrypsin and .alpha.1-antitrypsin. As measured by electroimmunoassay, the level of .alpha.1-antichymotrypsin in day 1 colostrum was higher than that in normal serum. Trace amounts of inter-.alpha.-trypsin inhibitor, .alpha.2-antiplasmin, .alpha.2-macroglobulin, antithrombin III or antileukoprotease could be demonstrated. According to their protease inhibiting activity, the 53 milk samples from day 1-3 could be divided into 2 groups. Presence of protease inhibiting activity (n = 35). Both .alpha.1-antitrypsin and .alpha.1-antichymotrypsin appeared intact and were able to form complexes with added trypsin or chymotrypsin although the major part of .alpha.1-antichymotrypsin showed a retarded electrophoretic mobility. The proteolytic activity was undetectable or low in these samples. No protease inhibiting activity, in spite of the presence of immunoreactive inhibitors (n = 18). .alpha.1-Antichymotrypsin had a precipitate pattern similar to group 1, while .alpha.1-antitrypsin had a major fraction with slightly retarded mobility and 2 minor peaks in the .alpha.1 and .beta.-regions. These precipitate patterns were unchanged on addition of human trypsin or chymotrypsin compatible with the presence of nonreactive inhibitor only. These samples had a caseinolytic and esterolytic activity with an electrophoretic mobility in the .beta.-region. All samples from day 4 and later had a demonstrable protease inhibiting activity.