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从小鼠肾脏中高产率快速纯化鸟氨酸脱羧酶并制备单克隆抗体。

Very fast purification of ornithine decarboxylase with high yield from mouse kidney and generation of a monoclonal antibody.

作者信息

Kopitz J, Adam G, Bohley P

机构信息

Physiologisch-Chemisches Institut, Universität Tübingen.

出版信息

Biol Chem Hoppe Seyler. 1990 Apr;371(4):363-8. doi: 10.1515/bchm3.1990.371.1.363.

Abstract

Based on methods for ornithine-decarboxylase purification published previously we developed an improved procedure for purification of the enzyme from the kidneys of testosterone-treated NMRI mice. Advantages of the new procedure are, that inactivation of the enzyme during purification is largely reduced by fast methods for purification and by the use of proteinase inhibitors. That way we got pure ornithine decarboxylase within 60 h with a yield of about 70%. A part of the highly purified ornithine decarboxylase was used for the generation of monoclonal antibodies.

摘要

基于先前发表的鸟氨酸脱羧酶纯化方法,我们开发了一种改进的程序,用于从经睾酮处理的NMRI小鼠的肾脏中纯化该酶。新程序的优点是,通过快速纯化方法和使用蛋白酶抑制剂,大大减少了纯化过程中酶的失活。通过这种方式,我们在60小时内获得了纯度较高的鸟氨酸脱羧酶,产率约为70%。一部分高度纯化的鸟氨酸脱羧酶用于制备单克隆抗体。

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