ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTEstradiol and progesterone binding to a fraction of ovine endometrial cytoplasmPaula E. Zimmering, Ilse Kahn, and Seymour LiebermanCite this: Biochemistry 1970, 9, 12, 2498–2506Publication Date (Print):June 9, 1970Publication History Published online1 May 2002Published inissue 9 June 1970https://doi.org/10.1021/bi00814a016RIGHTS & PERMISSIONSArticle Views16Altmetric-Citations7LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (967 KB) Get e-Alerts Get e-Alerts
Antisera that block the biological effects of estradiol-17β were produced by immunizing sheep with estradiol-17β-succinylbovine serum albumin. When administered up to 15 hr prior to the expected time of LH release, antiserum to estradiol-17β (anti-E2) blocked ovulation in PMS-treated immature rats. Ovulation was restored in animals receiving PMS and anti- E2 by the administration of HCG, indicating that the responsiveness of the ovaries to gonadotropingonadotropin was unaffected by the antiserum, and that therefore the antiserum acts by suppressing LH release. Replacement of the “blocked” endogenous estrogen with diethylstilbestrol, a synthetic estrogen whose activity is not inhibited anti-E2, restored ovulation in 3–040% of the animals treated with anti-E2 and PMS. These experiments offer direct evidence for the existence of a positive feedback role of estrogens the release of LH. (Endocrinology84: 893, 1969)
FERIN, MICHEL; ZIMMERING, PAULA E.; LIEBERMAN, SEYMOUR; VANDE WIELE, RAYMOND L. Author Information
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTBinding of Steroids to Steroid-Specific Antibodies*Paula E. Zimmering, Seymour Lieberman, and Bernard F. ErlangerCite this: Biochemistry 1967, 6, 1, 154–164Publication Date (Print):January 1, 1967Publication History Published online1 May 2002Published inissue 1 January 1967https://pubs.acs.org/doi/10.1021/bi00853a026https://doi.org/10.1021/bi00853a026research-articleACS PublicationsRequest reuse permissionsArticle Views102Altmetric-Citations16LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
Summary Antibodies to testosterone have been produced by immunization of ewes with conjugates of testosterone-17-hemisuccinate and bovine serum albumin suspended in Freund's complete adjuvant. Antibody has been separated from the sera by salt fractionation to obtain the globulin fraction, by dissolution of specific precipitates using a hapten analogue and by chromatography on DEAE-cellulose. The apparent specific precipitability of the antisera, and of all antibody-containing solutions derived from them, was markedly dependent on concentration. Our data can be expressed by the equation Aapp = A1 e-b(f-1) where Aapp is the apparent antibody titer at the dilution tested, A1 is the antibody titer of the undiluted test solution for which f = 1, f is the dilution factor, and b is a parameter which measures the degree of variation of precipitation of antibody with dilution. The concentration effect is probably not due to the solubility of antigen-antibody aggregates or to the changed configuration of proteins in dilute solution. It may be due to the presence of relatively weakly bound antibody molecules, or, more probably, to an increased possibility of intra-particulate interaction on dilution. The preferred method for specific purification of anti-testosterone antibodies was precipitation by heterologous antigen and dissolution of the precipitate by the hapten analogue, N,N-dimethylaminoethyl- 17β-(3-keto-4-androstenyl)-carbonate, followed by separation of the antibodies on Sephadex G-25. Two of the six ewes immunized produced antibodies which were bound by DEAE-cellulose, and which, when eluted, differed from unbound antibodies in that their specific precipitation by homologous antigen was inhibited by albumin or by some component associated with albumin.
Polycarboxylic acids containing a small number of p-nitrophenyl ester or p-nitroanilide groups were prepared and the pH dependence of their hydrolysis rates was investigated. The ester hydrolysis was found to be strongly catalyzed by an ionized carboxyl attached to the γ-carbon, resulting in an acceleration of the hydrolysis rate by a factor of about 106 at pH 5–6. The hydrolysis of p-nitroanilide groups was apparently affected little by one carboxylate in the γ position, but it was effectively inhibited when the carboxyls attached to both γ-carbons were ionized.