斑節蝦眼中穀胱甘?轉換?θ與皮質酮結合的探討

Abstract

用S-hexylglutathione吸附性管膠與陰離子交換管膠Mono Q可將斑節蝦眼睛的GST θ和GST ?分離。比較GSTθ與GST ?的相對含量以眼睛和鰓最高，神經次之。根據SDS-PAGE、SuperoseTM-12的証據，顯示GST θ為二聚體(Diner)，分子量約為50KDa，能與Corticosterone結合。經SDS-PAGE分析可結合在單元體(monomer)上，並能以10 mM 的Glutathione影響GSTθ與Corticosterone間的結合。老鼠的蛋白質激?C(PKC)、可使斑節蝦GSTθ進行磷酸化，但是，斑節蝦的蛋白質激?C無法使斑節蝦的GST磷酸化。

Two anionic isoenzymes of glutathione S transferase (EC 2.5.1.18), GSTθand GST ?，have been purified from the eyes of the shrimp Penaeus japonicus by using a combination of S-hexylglutathione affinity column chronmatography and Mono Q fast protein liquid chromatography (f.p.l.c.). The purified GST θ was a dimeric enzyme protein with subunit Mr abount 25 kDa. HPLC reverse phase C4 column analysis of various shrimp tissues indicated that the ratio of GSTθ vs. GST ? was highest in the eye and gi11. HPLC reverse phase C4 column analysis demostrated that corticosterone was selective binding to GST θ. Glutathione influenced the binding of corticosterone to the GST θ.