Del Boccio G, Di Ilio C, Casalone E, Pennelli A, Aceto A, Sacchetta P, Federici G
Ital J Biochem. 1987 Jan-Feb;36(1):8-17.
An anionic (pI 4.6) isoenzyme of glutathione transferase was purified to homogeneity from human thyroid by affinity chromatography followed by isoelectric focusing. The content of enzyme was calculated to constitute about 0.2% of soluble proteins. The enzyme is formed by two identical subunits of 23,000 daltons approximately. The thyroid transferase did not catalyze the reduction of peroxides. Physical, catalytic and immunological analyses demonstrated extensive similarities between the thyroid transferase and the transferase from placenta, erythrocytes and breast. On the other hand, the thyroid transferase appears catalytically different from transferase 7-7, even if both cross-react with the antibodies raised against human placenta transferase.
通过亲和层析继以等电聚焦，从人甲状腺中纯化出一种阴离子型（等电点4.6）谷胱甘肽转移酶同工酶，达到了均一性。经计算，该酶含量约占可溶性蛋白质的0.2%。该酶由两个约23,000道尔顿的相同亚基组成。甲状腺转移酶不催化过氧化物的还原反应。物理、催化和免疫学分析表明，甲状腺转移酶与来自胎盘、红细胞和乳腺的转移酶之间存在广泛相似性。另一方面，甲状腺转移酶在催化作用上似乎与转移酶7-7不同，即便二者都能与针对人胎盘转移酶产生的抗体发生交叉反应。
