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2-乙酰氨基芴诱导的大鼠肝癌中醛脱氢酶的纯化及免疫化学特性分析

Purification and immunochemical characterization of aldehyde dehydrogenase from 2-acetylaminofluorene-induced rat hepatomas.

作者信息

Lindahl R, Feinstein R N

出版信息

Biochim Biophys Acta. 1976 Dec 8;452(2):345-55. doi: 10.1016/0005-2744(76)90184-4.

Abstract
  1. A series of aldehyde dehydrogenase isozymes (aldehyde:NAD (P)+ oxidoreductase, EC 1.2.1.5), has been purified from hepatomas induced in Sprague-Dawley rats by 2-acetylaminofluorene. 2. The functional hepatoma-specific aldehyde dehydrogenase isozymes exist as 105 000-dalton dimers composed to two subunits of 53 000 daltons. Isoelectric points of the purified isozymes are 6.9-7.2. 3. Antiserum to these purified hepatoma-specific aldehyde dehydrogenases has been produced and the immunological relationships of these isozymes to their normal liver counterpart have been studied. Results of Ouchterlony double diffusions, agar-gel immunoelectrophoresis and polyacrylamide gel and agar immunoelectrophoresis indicate that anti-hepatoma aldehyde dehydrogenase antiserum cross-reacts with normal liver aldehyde dehydrogenase.
摘要
  1. 从用2-乙酰氨基芴诱导的斯普拉格-道利大鼠肝癌中,已纯化出一系列醛脱氢酶同工酶(醛:NAD(P)+氧化还原酶,EC 1.2.1.5)。2. 功能性肝癌特异性醛脱氢酶同工酶以由两个53000道尔顿亚基组成的105000道尔顿二聚体形式存在。纯化同工酶的等电点为6.9 - 7.2。3. 已制备了针对这些纯化的肝癌特异性醛脱氢酶的抗血清,并研究了这些同工酶与其正常肝脏对应物的免疫关系。琼斯特双扩散、琼脂凝胶免疫电泳以及聚丙烯酰胺凝胶和琼脂免疫电泳结果表明,抗肝癌醛脱氢酶抗血清与正常肝脏醛脱氢酶发生交叉反应。

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