使用胆囊收缩素衍生物或酸性氨基酸聚合物作为底物时脑酪氨酸硫酸转移酶活性的明显一致性。

Apparent identity of cerebral tyrosylsulfotransferase activities using either a cholecystokinin derivative or an acidic amino acid polymer as substrate.

作者信息

Vargas F, Schwartz J C

出版信息

FEBS Lett. 1987 Jan 26;211(2):234-8. doi: 10.1016/0014-5793(87)81443-6.

Abstract

The tyrosylsulfotransferase activities of rat cerebral fractions transferring [35S]sulfate groups from 3'-phosphoadenosine 5'-[35S]phosphosulfate to either Boc-cholecystokinin-8 (in non-sulfated form) or the acidic amino acid polymer (Glu, Ala, Tyr)n (6:3:1) were compared. They appear similar regarding subcellular distribution (both being enriched in the microsomal fraction) and inhibition by an excess of the acidic amino acid polymer, NaCl or 2,6-dichloro 4-nitrophenol. These results obtained with artificial substrates suggest that identical (or closely similar) tyrosylsulfotransferases are responsible for sulfation of tyrosine residues of several secretory proteins from various tissues.

摘要

比较了大鼠脑部分的酪氨酰硫酸转移酶活性，该酶将[35S]硫酸基团从3'-磷酸腺苷5'-[35S]磷酸硫酸转移至Boc-缩胆囊素-8（非硫酸化形式）或酸性氨基酸聚合物（Glu，Ala，Tyr）n（6:3:1）。它们在亚细胞分布方面（均在微粒体部分富集）以及被过量酸性氨基酸聚合物、NaCl或2,6-二氯-4-硝基苯酚抑制方面表现相似。这些使用人工底物获得的结果表明，相同（或非常相似）的酪氨酰硫酸转移酶负责多种组织中几种分泌蛋白酪氨酸残基的硫酸化。