Protease inhibitors in tracheobronchial secretions.

Protease inhibitors in tracheobronchial secretions.
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气管支气管分泌物中的蛋白酶抑制剂。

DOI:
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发表时间:
1983
期刊:
Journal of Laboratory and Clinical Medicine
影响因子:
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通讯作者:
B. Bromke
B. Bromke
中科院分区:
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文献类型:
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作者:
F. Kueppers;B. Bromke

文献摘要

被引文献

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从气管支气管分泌物中分离并鉴定了三种蛋白酶抑制剂。作为起始材料,使用气管造口患者的合并分泌物。分离程序包括用3%高氯酸沉淀(主要的酸稳定抑制剂保留在溶液中),胰蛋白酶-琼脂糖凝胶亲和层析和制备区带电泳。我们发现了三种不同的抑制剂。一种是碱性蛋白,具有大小和电荷异质性的证据,但具有免疫学同质性,Mr = 15,850 +/- 1200道尔顿,12,600 +/- 700,6500 +/- 500。两种抑制剂是酸性蛋白质,Mr = 63,400 +/- 3200(AI)和19,960 +/- 1500(AII)道尔顿。碱性抑制剂具有酪氨酸作为唯一的氨基末端氨基酸。两种酸性抑制剂均未发现氨基末端,三种抑制剂均含有中性糖和氨基糖,但不含唾液酸。抑制胰蛋白酶、胰凝乳蛋白酶和人粒细胞弹性蛋白酶。这两种酸性抑制剂在免疫学上是相关的;它们显然来自血清ITI。抑制剂AII来源于抑制剂AI,可能是通过几种蛋白酶的有限蛋白水解。42例阻塞性肺疾病患者支气管分泌物中碱性抑制物的浓度为0.206 ± 0.15 mg/ml。
The isolation and characterization of three protease inhibitors from tracheobronchial secretions are described. As starting material, pooled secretions from patients with tracheostomies was used. The isolation procedure consisted of precipitation with 3% perchloric acid (the major acid-stable inhibitors remain in solution), affinity chromatography on trypsin-Sepharose, and preparative zone electrophoresis. We found three distinct inhibitors. One was a basic protein with evidence of size and charge heterogeneity but immunologic homogeneity, Mr = 15,850 +/- 1200 daltons, 12,600 +/- 700, 6500 +/- 500. Two inhibitors were acidic proteins, Mr = 63,400 +/- 3200 (AI) and 19,960 +/- 1500 (AII) daltons. The basic inhibitor had tyrosine as the sole aminoterminal amino acid. For the two acidic inhibitors, an aminoterminus was not found. All three inhibitors contained neutral sugars and amino sugars but no sialic acid. They inhibit trypsin, chymotrypsin, and human granulocytic elastase. The two acidic inhibitors are immunologically related; they are apparently derived from serum ITI. Inhibitor AII originates from inhibitor AI, probably by limited proteolysis by several proteases. The concentration of the basic inhibitor in bronchial secretions of 42 patients with obstructive lung disease was 0.206 +/- 0.15 mg/ml.