STRUCTURAL AND FUNCTIONAL-CHARACTERIZATION OF THE ABNORMAL Z-ALPHA1-ANTITRYPSIN ISOLATED FROM HUMAN-LIVER
STRUCTURAL AND FUNCTIONAL-CHARACTERIZATION OF THE ABNORMAL Z-ALPHA1-ANTITRYPSIN ISOLATED FROM HUMAN-LIVER
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DOI：
10.1016/0014-5793(84)81279-x
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发表时间：
1984-01-01
期刊：
影响因子：
3.5
通讯作者：
CARRELL, RW
中科院分区：
文献类型：
--
作者：
BATHURST, IC;TRAVIS, J;CARRELL, RW
α1-抗胰蛋白酶已从纯合 Z 缺陷受试者的肝脏包涵体中分离出来。通过在 pH 2.0 或 pH 8.0 的高盐中萃取，可以将抑制剂恢复为完全活性的形式。碳水化合物分析表明蛋白质处于“高甘露糖”形式，这与其对内切-βN-氨基葡萄糖苷酶的敏感性相配合。这些数据表明，异常的α1-抗胰蛋白酶在进入高尔基体之前在分泌途径中被阻断，并且这种阻断不是由于多肽的严重错误折叠所致。α1-抗胰蛋白酶人肝脏包涵体高甘露糖蛋白蛋白酶抑制剂
α1-Antitrypsin has been isolated from liver inclusion bodies of a subject with a homozygous Z deficiency. The inhibitor was recovered in a fully active form by extraction in high salt at either pH 2.0 or pH 8.0. Carbohydrate analysis indicated a protein in the ‘high mannose’ form, and this was collaborated by its sensitivity to endo-βN-glucosaminidase. These data suggest that the abnormal α1-antitrypsin is blocked in the secretory pathway prior to its entrance into the Golgi, and that this blockage is not due to a gross misfolding of the polypeptide.α1-AntitrypsinHuman liverInclusion bodyHigh mannose glycoproteinProteinase inhibitor