翡翠贻贝(Perna viridis)谷胱甘肽硫转移酶同工酶的分离纯化及部分性质研究

以翡翠贻贝（Perna viridis）消化腺为材料,经GST rap^TMFF柱亲和层析,分离纯化得到总谷胱甘肽硫转移酶。而后经DEAE离子交换层析得到三个洗脱峰M₁、M₂、M₃,分别占总蛋白含量的77%,16%,2.9%,对其进行SDS-PAGE分析,结果表明M₁可能是由分子量为25 kD的蛋白质亚基组成的同型二聚体,M₂、M₃可能为异型二聚体,M₂由25 kD和23kD两个亚基组成,M₃由27kD和23kD两个亚基组成。以1-氯-2,4-二硝基苯（CDNB）、3,4-二氯硝基苯（DCNB）、4-硝基氯化苄（NBC）、利尿酸（ETHA）4种底物对M₁、M₂、M₃进行动力学分析,发现M₁、M₂、M₃分别对ETHA、DCNB、NBC亲和力更好,Km分别为1.08mmol/L、1.51 mmol/L、0.89mmol/L,Vmax分别为54.9μmol/min/mg,40.3μmol/min/mg,19.4μmol/min/mg。

Purification and Partial Characterization of the Glutathione S-transferase Isozymes from the mussel , Perna viridis

Total glutathione S-transferases were purified from digestive gland of mussel(Perna viridis) by GST rap FF.Then three glutathione S-transferase isozymes(M_1,M_2,M_3) were purified and separated with ion exchange chromatography.SDS-PAGE analysis of glutathione S-transferase isozymes(M_1,M_2,M_3) indicated that M_1 may be a single homodimer and the molecular weight of M_1 is 25 kD,while M_2 and M_3 may be two heterodimers,M_2 showed two bands and the molecular weight of the subunits are 25 kD and 23 kD respec...