贻贝过氧化氢酶的纯化及部分性质

【摘要】 新鲜贻贝肉匀浆抽提液经硫酸铵盐析、DEAE-Sepharose FF柱层析纯化，得到一种过氧化氢酶。该酶为糖蛋白，亚基分子量约为76000，中性糖含量约为10.56%，研究结果表明，贻贝过氧化氢酶的最佳pH7.0左右，对热不稳定，45℃保温15min，酶的残余活力约为70%；60℃保温15min，则酶的残余活力仅剩10.6%左右。NaN3、KCN及某些金属离子如Pb2+、Hg2+、Fe2+、Cd2+等抑制酶的活性；Zn2+、Cu2+、Mg2+则对酶有不同程度的激活作用。更多还原

【Abstract】 A catalase from fresh Perna Viridis had been purified by the use of saline extraction,ammonium sulfate precipition and DEAE-Sepharose FF column chromatography.It was identified as glycoprotein and the neutral saccharide content of the enzyme was assayed as about 1056% .The enzyme subunit molecular weight was about 76000 as determined by SDS-polyacrylamide gel electrophoresis.The experiment result indicated that the optimal temperatme and pH of the enzyme were 35℃ and 7 respectively.The enzyme was not stable in heat and retained 70% of the original enzyme activity after incubation at 45℃ for 15min .It had only 10.6% of the original enzyme activity after incubation at 60℃ for 15min .Its catalytic activity was strongly inhibited by NaN3 and KCN The metal ions Pb2+、Hg2+、Fe2+、Cd2+ 、Ni2+ showed some inhibition and Zn2+、Cu2+、Mg2+ could increase its activity in varying degrees.更多还原