Orekhovich V N, Firfarova K F, Strizhevskaia E M
Biokhimiia. 1975 Jul-Aug;40(4):833-7.
Four highly purified enzyme preparations, which belongs to the cathepsine A group in their substrate specificity, are isolated from the extract of a hen liver acetone powder. The preparations are designated as A1, A2, A3 and A4 according to their electrophoretic mobility. The A1 component is a protein with molecular weight of about 200 000, it degrades a synthetic substrate and, to a small degree, hemoglobin. This protein is suggested to be the fragment of a liver enzyme complex. The A2 component has molecular weight of about 70 000 and the highest activity. The A3 component has molecular weight 100 000 and the lowest activity. The A2 and A3 components are similar to cathepsine A from other tissues. THe A4 component is characterized by a high electrophoretic mobility, a resistance in neutral and weakly alkaline media and a low molecular weight (of about 60 000). Cu2+, Ag+ and diisopropylphosphofluoridate completely inhibited the activity of all the enzyme preparation studied. Tosyl-alpha-amino-phenylethyl-chloremethylketone inhibited the enzymes activity only by 50-70%.
从鸡肝丙酮粉提取物中分离出四种高度纯化的酶制剂，它们在底物特异性上属于组织蛋白酶A组。根据电泳迁移率，这些制剂被命名为A1、A2、A3和A4。A1组分是一种分子量约为200000的蛋白质，它能降解一种合成底物，并在一定程度上降解血红蛋白。这种蛋白质被认为是肝酶复合物的片段。A2组分分子量约为70000，活性最高。A3组分分子量为100000，活性最低。A2和A3组分与其他组织中的组织蛋白酶A相似。A4组分的特点是电泳迁移率高、在中性和弱碱性介质中具有抗性且分子量低（约为60000）。铜离子、银离子和二异丙基磷酰氟化物完全抑制了所有研究的酶制剂的活性。甲苯磺酰-α-氨基苯乙基氯甲基酮仅使酶活性抑制50-70%。
