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首页> 外文期刊>Preparative biochemistry & biotechnology: An international journal for rapid communication >Purification of turnip peroxidase and its kinetic properties
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Purification of turnip peroxidase and its kinetic properties

机译：萝卜过氧化物酶的纯化及其动力学性质

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摘要

Peroxidase from turnip roots was purified using metalaffinity chromatography up to a specific activity of 337 units/mg protein with 3.02 RZ and 63.5% recovery.After purification,the enzyme showed 2-3 bands on sodium dodecyl sulphate polyacrylamide gel electrophoresis .The molecular weight of the purified enzyme was found to be 37-39 kD with matrix assisted laser desorption ionization mass spectrometer .The enzyme showed maximum activity in phosphate buffer,pH 6.0,and lowest activity in borate buffer at the same pH.The K_m of the enzyme was found to be 7.07*10~9-4) mM.Turnip peroxidase also contains anironmoiety which is found to be about 0.28%.The enzyme showed 50% inhibition of its specific activity with ethylene diamine tetraacetic acid (EDTA).
机译：用金属亲和色谱法纯化萝卜根部的过氧化物酶，使其比活度达到337单位/ mg蛋白，RZ为3.02，回收率63.5％。纯化后，该酶在十二烷基硫酸钠聚丙烯酰胺凝胶电泳中显示2-3条带。用基质辅助激光解吸电离质谱仪测定纯化的酶为37-39 kD。在相同pH下，该酶在磷酸盐缓冲液中的活性最高，pH 6.0，在硼酸盐缓冲液中的活性最低。约为7.07 * 10〜9-4）mM.Turnip过氧化物酶还含有约0.28％的铁基部分。该酶对乙二胺四乙酸（EDTA）的比活性具有50％的抑制作用。

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