Hiraiwa M, Yamauchi T, Tsuji S, Nishizawa M, Miyatake T, Oyanagi K, Ikuta F, Uda Y
Department of Health Chemistry, Niigata College of Pharmacy.
J Biochem. 1993 Dec;114(6):901-5. doi: 10.1093/oxfordjournals.jbchem.a124274.
An acid sialidase [EC 3.2.1.18], partially purified from human placenta by Con A-Sepharose adsorption and p-aminophenyl thio-beta-D-galactoside-CH-Sepharose (PATG-Sepharose) affinity chromatographies, was activated by incubation at 37 degrees C. This activation showed both time and temperature dependencies, with the most effective activation observed at 37 degrees C in the pH range between 4.3 and 5.2. The influence of various protease inhibitors on its activation was investigated. Among the protease inhibitors tested, amastatin, an inhibitor of aminopeptidase A, significantly inhibited activation. The partially purified enzyme preparation contained aminopeptidase activity, which was inhibited by amastatin. Zinc ions inhibited either the activation of sialidase or the aminopeptidase activity in the enzyme preparation. These results suggest the possibility of participation of aminopeptidase function in the activation process of sialidase.
通过Con A - 琼脂糖吸附和对氨基苯硫基 - β - D - 半乳糖苷 - CH - 琼脂糖（PATG - 琼脂糖）亲和层析从人胎盘中部分纯化得到的一种酸性唾液酸酶[EC 3.2.1.18]，在37℃孵育时被激活。这种激活表现出时间和温度依赖性，在37℃、pH值在4.3至5.2之间时观察到最有效的激活。研究了各种蛋白酶抑制剂对其激活的影响。在所测试的蛋白酶抑制剂中，氨肽酶A的抑制剂抑肽酶显著抑制激活。部分纯化的酶制剂含有氨肽酶活性，该活性被抑肽酶抑制。锌离子抑制唾液酸酶的激活或酶制剂中的氨肽酶活性。这些结果表明氨肽酶功能可能参与唾液酸酶的激活过程。
