| 摘要: |
| 采用分光光度法研究了环境因子对栉孔扇贝(Chlamys farreri)血淋巴中谷胱甘肽转硫酶(GST)活性的影响。结果表明, 血清和血细胞中都存在GST, 且血细胞中酶活力高于血清。血细胞中GST 的适宜温度范围是20～35℃, 最适温度为30℃, 在60℃时酶活力完全丧失。该酶的适宜pH 为7～8, 最适pH 为7.5。将血细胞裂解液在不同温度水浴中放置30 min 后, GST 的热稳定性随温度的升高而降低,35℃时的酶活力为20℃的22%, 显示该酶的热稳定性较差; 低温下该酶的稳定性也较差, 4℃存12 h 后酶活力丧失了51%。Cu2+和Pb2+对GST 活力有显著抑制作用, 在0～2.5 mg/L 质量浓度范围内, GST 活力随Cu2+质量浓度的升高而降低; 在0～5 mg/L 质量浓度范围内, GST 活力随Pb2+质量浓度的增大而下降。 |
| 关键词: 栉孔扇贝(Chlamys farreri) 血淋巴 谷胱甘肽转硫酶 酶活力 |
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| 基金项目:山东省自然科学基金项目(ZR2010CM017) |
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| The effect of environmental factors on the activities of glutathione S-transferases in haemolymph of scallop Chlamys farreri |
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| Abstract: |
| The activities and properties of glutathione S-transferases (GST) in the haemolymph of Chlamys farreri were assayed with the spectrophotometric method of 1-Chloro-2,4-dinitrobenzene (CDNB). Effects of pH, temperature, and heavy metal irons on the activities of GST in the haemocytes were studied. In addition, the thermal stability was also tested. GST activity was found in both serum and haemocytes of Chlamys farreri, and GST activity in the haemocytes was higher than that in the serum. The optimum temperature range of GST in the haemocytes was from 20℃ to 35℃, with the optimum temperature at 30℃. GST lost its activity completely at the temperature of 60℃. At pH ranging from 7 to 8, the GST in the haemocytes showed higher activities, with the optimum pH at 7.5. After the lysate of haemocytes was incubated at different temperatures for 30 min, the activities of GST in the haemocytes became descending with the increasing of temperature. The activities value of GST at 35℃ was only 22% of that at 20℃. Moreover, the activity of GST was very unstable even under low temperature. Being incubated at 4℃ for 12h, GST lost 51% of its activities. Cu2+ and Pb2+ could inhibit the activities of GST. When the concentration of Cu2+ was below 2.5mg/L or Pb2+ was below 5mg/L, the activities of GST was descending with the increasing of heavy metal irons concentration. |
| Key words: Chlamys farreri haemolymph gutathione s-transferases enzyme activities |
