Purification of human alpha uterine protein
| Autor: | R. MacKinnon, L. V. B. Nicholson, R. G. Sutcliffe, A. E. Bolton, F. Sharp |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Embryology
Dimer Size-exclusion chromatography Chromatography Affinity chemistry.chemical_compound Endocrinology Affinity chromatography Pregnancy Decidua Humans Uteroglobin Polyacrylamide gel electrophoresis Glycoproteins biology Chemistry Obstetrics and Gynecology Cell Biology Molecular Weight Electrophoresis Reproductive Medicine Biochemistry DEAE-Sepharose Sephadex Chromatography Gel biology.protein Electrophoresis Polyacrylamide Gel Female Antibody Immunoelectrophoresis Two-Dimensional |
| Zdroj: | Reproduction. 58:435-442 |
| ISSN: | 1741-7899 1470-1626 |
| DOI: | 10.1530/jrf.0.0580435 |
| Popis: | Summary. Human alpha uterine protein (AUP) has been prepared from extracts of decidua by antibody affinity chromatography, DEAE Sepharose chromatography and by filtration through Sephadex G-150. This procedure yielded a protein fraction containing AUP, which was labelled with 125I by chloramine T. When analysed by SDS gel electrophoresis this radioiodinated protein fraction was found to contain predominantly a single species of protein which was precipitated by antibodies against AUP in antibody\p=n-\antigencrossed electrophoresis. Rabbit anti-AUP precipitated 55\p=n-\65%of the tracer in a double-antibody system. Sephadex G150 gel filtration of AUP obtained before and after affinity chromatography provided a molecular weight estimate of 50 000. Since SDS gel electrophoresis revealed a polypeptide molecular weight of 23 000\p=n-\25000, it is suggested that AUP is a dimer. |
| Databáze: | OpenAIRE |
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