| Isolation of two forms of rat alpha-fetoprotein and comparison of their binding parameters with estradiol-17beta. | |
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MedLine Citation:
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PMID: 53073 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In polyacrylamide gels, highly purified rat alpha1-fetoprotein shows a molecular heterogeneity, i.e. a "slow" and a "fast" moving fraction. We have isolated by electrophoretic fractionation and subsequent elution these two forms of alpha1-fetoprotein, and we have studied comparatively the binding parameters for estradiol-17beta of whole alpha1-fetoprotein preparations and of the isolated forms. We have shown that the number of binding sites per molecule of whole alpha1-fetoprotein is always, in our experimental conditions, a fractional number, inferior to unity (0.3). Furthermore, the analysis of the binding parameters of the "two forms" of alpha1-fetoprotein allows discrimination between different classes of binding sites. For the "slow" fraction, the number of predominant binding sites per molecule of protein is close to unity (0.7-0.9), whereas for the "fast" fraction, a very low fractional value is found (0.1). The corresponding association constants are reproducibly different for the two fractions: Ka = 0.1.10(8) M-1 for the "slow" alpha1-fetoprotein, and Ka = 0.7.10(8) M-1 for the "fast" alpha1-fetoprotein. Traces of a very high affinity (10(9) M-1) minor class of binding sites are demonstrated in the "slow" fraction. These results point to the existence of a molecular population of alpha1-fetoprotein, some forms of which have a strong or very strong affinity, and some a negligible affinity, for estrogens. |
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Authors:
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C Benassayag; G Vallette; N Cittanova; E Nunez; M F Jayle |
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Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 412 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1975 Dec |
Date Detail:
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Created Date: 1976-02-09 Completed Date: 1976-02-09 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 295-305 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Binding Sites Carcinoma, Hepatocellular / blood Estradiol* Female Fetal Proteins* Liver Neoplasms / blood Male Protein Binding Protein Conformation Rats alpha-Fetoproteins* / immunology, isolation & purification |
| Chemical | |
Reg. No./Substance:
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0/Fetal Proteins; 0/alpha-Fetoproteins; 50-28-2/Estradiol |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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