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乳过氧物酶的分离提纯及其应用于蛋白质的碘化标记

Isolation and Purification of Lactoperoxidase and Its Application to the Radio-iodination of IgG

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【作者】 赵武述王世中傅莉成

【Author】 Zhao Wushu, Fu Licheng and Wang Shizhung Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences;National Institute for the Control of Pharmaceuticals and Biological Products

【机构】 中国医学科学院基础医学研究所卫生部生物制品及药品检定所 北京北京北京

【摘要】 本文介绍一种提取乳过氧化物酶的较简易方法。先用CM-SephadexC-50从牛奶中吸附出粗酶,再经硫酸铵分段盐析,最后用CM-纤维素柱纯化,所得酶制品的A412nm/A280nm比值可达0.95,比活性可达58.6GU/mg,产量常不低于5mg/L牛乳。此酶用于IgG的碘化标记,结果满意。

【Abstract】 A simplified method for the isolation and purification of lactoperoxi-dase was described. Lactoperoxidase in fresh milk was adsorbed with CM-Sephadex and then fractionated by ammonium sulfate. The crude enzyme was finally purified by CM-cellulose chromatography. The enzyme thus prepared is quite pure. Its A412nm/A280nm ratio usually exceeds 0.9 and its specific activity can be as high as 58.6 GU/mg. The enzyme yield is no less than 5 mg per liter of milk. Human IgG radio-iodinated with this enzyme preparation proved to be satisfactory.

  • 【文献出处】 中国医学科学院学报 ,Acta Academiae Medicinae Sinicae , 编辑部邮箱 ,1982年02期
  • 【被引频次】1
  • 【下载频次】66
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