1. The specificity of 3 oestradiol-binding proteins was studied. Two of these proteins are naturally occurring (rat α-foetoprotein and rat liver microsomal 17β-hydroxy steroid dehydrogenase) and the third is an artificially induced model, anti-(oestradiol-6-carboxymethyloxime-bovine serum albumin) γ-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 (α-foetoprotein and 17β-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 γ-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.
The comparative specificity of three oestradiol-binding proteins. Rat α-foetoprotein, rat liver 17β-hydroxy steroid dehydrogenase and anti-(oestradiol-6-carboxymethyloxime-bovine serum albumin) antiserum
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C Laurant, S D de Lauzon, N Cittanova, E Nunez, M F Jayle; The comparative specificity of three oestradiol-binding proteins. Rat α-foetoprotein, rat liver 17β-hydroxy steroid dehydrogenase and anti-(oestradiol-6-carboxymethyloxime-bovine serum albumin) antiserum. Biochem J 1 December 1975; 151 (3): 513–518. doi: https://doi.org/10.1042/bj1510513
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