Konishi-Imamura L, Dohi K, Sato M, Kobashi K
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University.
J Biochem. 1994 Jun;115(6):1097-100. doi: 10.1093/oxfordjournals.jbchem.a124463.
Arylsulfate sulfotransferase (ASST) from a human intestinal bacterium stoichiometrically catalyzed the transfer of the sulfate group of phenylsulfate esters to phenolic compounds. Polyclonal antibodies against ASST were obtained from rabbit sera. These antisera did not inhibit ASST activity. ASST was recognized by the IgG fraction of the antisera, but rat liver phenol sulfotransferase did not show cross-reactivity to ASST on Western blot (immunoblot) analysis. The ASST was purified by an anti-ASST immobilized affinity column chromatography to homogeneity on SDS-PAGE. The NH2-terminal amino acid and partial sequence of the purified enzyme were serine and SVKYSFEDHIINRQYEAEQAMLAKF, respectively. We corrected the previous result that the NH2-terminal of ASST was arginine.
来自一种人类肠道细菌的芳基硫酸酯硫酸转移酶（ASST）以化学计量方式催化硫酸苯酯的硫酸基团向酚类化合物的转移。从兔血清中获得了针对ASST的多克隆抗体。这些抗血清不抑制ASST活性。ASST可被抗血清的IgG组分识别，但在蛋白质印迹（免疫印迹）分析中，大鼠肝脏酚硫酸转移酶与ASST未显示交叉反应性。通过抗ASST固定化亲和柱色谱法将ASST纯化至SDS-PAGE上的均一性。纯化酶的NH2末端氨基酸和部分序列分别为丝氨酸和SVKYSFEDHIINRQYEAEQAMLAKF。我们纠正了之前关于ASST的NH2末端为精氨酸的结果。
