三种雌二醇结合蛋白的相对特异性。大鼠甲胎蛋白、大鼠肝脏17β-羟基类固醇脱氢酶及抗（雌二醇-6-羧甲基肟-牛血清白蛋白）抗血清。
The comparative specificity of 3 oestradiol-binding proteins. Rat alpha-foetoprotein, rat liver 17beta-hydroxy steroid dehydrogenase and anti-(oestradiol-6-carboxymethyloxime-bovine serum albumin) antiserum.
作者信息
Laurant C, de Lauzon S D, Cittanova N, Nunez E, Jayle M F
出版信息
Biochem J. 1975 Dec;151(3):513-8. doi: 10.1042/bj1510513.
Abstract
- The specificity of 3 oestradiol-binding proteins was studied. Two of these proteins are naturally occurring (rat alpha-foetoprotein and rat liver microsomal 17beta-hydroxy steroid dehydrogenase) and the third is an artificially induced model, anti-(oestradiol-6-carboxymethyloxime-bovine serum albumin) gamma-globulins. 2. A specific binding procedure for each protein model permitted a determination of its affinity for oestradiol and for 30 other steroids. 3. The results obtained have brought to light the different areas of the steroid molecule that are important for its recognition by each of the three proteins. The two naturally occurring proteins (alpha-foetoprotein and 17beta-hydroxy steroid dehydrogenase) recognize the edge of the steroid defined by C-4, C-6, C-8 and C-15. On the other hand, the gamma-globulins recognize the opposite edge, i.e. that defined by C-2, C-10, C-11 and C-17. 4. Diethylstilboestrol, whose structure is analogous to that of a steroid, is only recognized by the two naturally occurring proteins.
摘要
- 对三种雌二醇结合蛋白的特异性进行了研究。其中两种蛋白是天然存在的（大鼠甲胎蛋白和大鼠肝脏微粒体17β-羟基类固醇脱氢酶），第三种是人工诱导的模型，即抗（雌二醇-6-羧甲基肟-牛血清白蛋白）γ-球蛋白。2. 针对每种蛋白模型的特异性结合程序，可测定其对雌二醇和其他30种类固醇的亲和力。3. 所得结果揭示了类固醇分子中对三种蛋白各自识别重要的不同区域。两种天然存在的蛋白（甲胎蛋白和17β-羟基类固醇脱氢酶）识别由C-4、C-6、C-8和C-15界定的类固醇边缘。另一方面，γ-球蛋白识别相对的边缘，即由C-2、C-10、C-11和C-17界定的边缘。4. 己烯雌酚，其结构类似于类固醇，仅被两种天然存在的蛋白识别。
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引用本文的文献
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Rat alpha-foetoprotein. Purification, physicochemical characterization, oestrogen-binding properties and chemical modification of the thiol group.
Biochem J. 1978 Oct 1;175(1):73-81. doi: 10.1042/bj1750073.
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