Slight differences between adenosine deaminases from different species an immunochemical study.

J J Centelles, R Franco
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引用次数: 0

Abstract

IgGs against adenosine deaminase from rat brain, rat liver, mouse duodenum and human erythrocyte were purified from rabbit antisera with yields of 82-87%. The inhibition of adenosine deaminase by the antienzyme is studied, and it is demonstrated that rat and mouse antibodies are tight-binding inhibitors. These antibodies inhibit either the rat or the mouse enzymes and do not inhibit the human erythrocytes enzyme. The human antibody does not inhibit either the human or the rat or mouse enzyme. These results indicate that some differences in antigenic behaviour near the active site must be encountered among species. Comparing the sequenced of the two products corresponding to two adenosine deaminase genes recently sequenced (human and murine) a hypothesis concerning the localization of the adenosine deaminase active site is proposed.

不同物种的腺苷脱氨酶之间的细微差异:免疫化学研究。
从兔抗血清中纯化了来自大鼠脑、大鼠肝脏、小鼠十二指肠和人红细胞的抗腺苷脱氨酶igg,产率为82 ~ 87%。研究了该抗酶对腺苷脱氨酶的抑制作用,并证明了大鼠和小鼠抗体是紧密结合抑制剂。这些抗体抑制大鼠或小鼠的酶,不抑制人红细胞酶。人抗体不抑制人或大鼠或小鼠的酶。这些结果表明,在不同的物种之间,在活性位点附近的抗原行为一定存在一些差异。通过比较最近测定的两种腺苷脱氨酶基因(人和鼠)对应的两种产物的序列,提出了腺苷脱氨酶活性位点定位的假设。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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