兔肝脏的溶酶体酸性蛋白酶。
Lysosomal acid proteinase of rabbit liver.
作者信息
Barrett A J
出版信息
Biochem J. 1967 Aug;104(2):601-8. doi: 10.1042/bj1040601.
Abstract
- Acid proteinase from rabbit liver lysosomes was purified about 1000-fold, on a protein basis. 2. The purification procedure involved isolation of a lysosomal-mitochondrial pellet and conversion of this into an acetone-dried powder. 3. The enzyme was extracted with an acidic buffer and subjected to column chromatography with DEAE-Sephadex and Sephadex G-100. 4. The molecular weight of the enzyme was 50000-52000. 5. Maximal activity against haemoglobin was obtained at pH3.2; serum albumin was attacked, but very much more slowly. 6. Several possible inhibitors of the enzyme were tested. Thiol-blocking reagents, several inhibitors of trypsin and chymotrypsin, and a chelating agent were without effect. 7. The enzyme was competitively inhibited by 3-phenylpyruvic acid at low concentrations. 8. Dithiothreitol caused rapid inactivation of the enzyme at pH8. 9. It is concluded that this enzyme is a form of cathepsin D, which may be widely distributed in lysosomes.
摘要
- 以蛋白质计，兔肝脏溶酶体中的酸性蛋白酶被纯化了约1000倍。2. 纯化过程包括分离溶酶体 - 线粒体沉淀并将其转化为丙酮干粉。3. 用酸性缓冲液提取该酶，并进行DEAE - 葡聚糖凝胶和葡聚糖凝胶G - 100柱色谱。4. 该酶的分子量为50000 - 52000。5. 在pH3.2时对血红蛋白的活性最高；血清白蛋白也会被作用，但速度要慢得多。6. 测试了几种该酶可能的抑制剂。巯基阻断剂、几种胰蛋白酶和胰凝乳蛋白酶抑制剂以及一种螯合剂均无作用。7. 在低浓度下，3 - 苯基丙酮酸对该酶有竞争性抑制作用。8. 二硫苏糖醇在pH8时会使该酶迅速失活。9. 得出结论，这种酶是组织蛋白酶D的一种形式，可能广泛分布于溶酶体中。
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