2010•China Forestry Science and TechnologyRequires access
Partial purification of glutathione S-transferases by protein precipitators in Micromelalopha troglodyta(Lepidoptera:Notodontidae)
Xueyan Shi
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Abstract
The partial purification of glutathione S-transferases(GSTs) in the larvae of Micromelalopha troglodyta was studied using ammonium sulfate fractionation and polyethyleneglycol(PEG) fractionation.The results showed that the peak of GST activity was in 40%~60% of ammonium sulfate fractionation,and the specific activity was 174.41 nmol/(min·mg),and the purification factor was 1.39 fold.The efficacy of purification by PEG20000 was the best in five kinds of PEG tested.By the PEG20000 fractionation,the activity peak of GSTs was in 10%~15%,the specific activity was 454.14 nmol/(min·mg),and purification factor was 15.50 fold.Therefore,the efficacy of GST purification by PEG20000 was better than that of ammonium sulfate fractionation in M.troglodyta.