大鼠肝脏溶酶体芳基酰胺酶的一些特性
Some properties of lysosomal arylamidase in rat liver.
作者信息
Hiroi Y, Toku S
机构信息
Department of Nutritional Chemistry, Nakamura Gakuen College, Fukuoka, Japan.
出版信息
Biochem Mol Biol Int. 1993 Jul;30(4):705-11.
Lysosomal arylamidase in rat liver was reassessed. The arylamidase was distinguishable into seven types having different isoelectric points by isoelectric fractionation. All the types hydrolyzed valine beta-naphthylamide most rapidly among amino acid beta-naphthylamides tested, but did not hydrolyze arginine beta-naphthylamide. These enzymes exhibited maximum activities at pH 7.0. They had a molecular weight of 135,000 by gel filtration on a Sephacryl S-200. They were all inhibited by sulfhydryl-blocking reagents and activated by sulfhydryl compounds, indicating to be cysteine proteases.
对大鼠肝脏中的溶酶体芳基酰胺酶进行了重新评估。通过等电分级分离，该芳基酰胺酶可分为七种具有不同等电点的类型。在测试的氨基酸β-萘酰胺中，所有类型对缬氨酸β-萘酰胺的水解速度最快，但不水解精氨酸β-萘酰胺。这些酶在pH 7.0时表现出最大活性。通过在Sephacryl S-200上进行凝胶过滤，它们的分子量为135,000。它们均被巯基封闭试剂抑制，并被巯基化合物激活，表明它们是半胱氨酸蛋白酶。
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