Suiko M, Tojo T, Fernando P H, Sakakibara Y, Kawano J, Liu M C
Department of Biological Resource Sciences, Miyazaki University, Japan.
Biosci Biotechnol Biochem. 1996 Jan;60(1):137-8. doi: 10.1271/bbb.60.137.
Three mammalian and eight non-mammalian arylsulfatases were investigated for their activities toward tyrosine-O-sulfate (TyrS) in peptides. None of the mammalian arylsulfatases exhibited detectable activities toward TyrS-containing peptides. Of the non-mammalian arylsulfatases tested, Types VII, VIII, and H-1, 2, and 5 displayed strong activity on endo-TyrS residues. The prokaryotic sulfatase, Type VI, was active only on free TyrS and N-terminal TyrS of Leu-enkephalin. All the sulfatases were active on p-nitrophenyl sulfate and p-nitrocatechol sulfate.
研究了三种哺乳动物和八种非哺乳动物芳基硫酸酯酶对肽中酪氨酸-O-硫酸盐（TyrS）的活性。没有一种哺乳动物芳基硫酸酯酶对含TyrS的肽表现出可检测到的活性。在所测试的非哺乳动物芳基硫酸酯酶中，VII型、VIII型以及H-1、2和5型对内源TyrS残基具有强活性。原核硫酸酯酶VI型仅对亮氨酸脑啡肽的游离TyrS和N端TyrS有活性。所有硫酸酯酶对硫酸对硝基苯酯和硫酸对硝基邻苯二酚均有活性。
