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Purification of human alpha uterine protein

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 with¹²⁵I 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–antigen crossed electrophoresis. Rabbit anti-AUP precipitated 55–65% 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 23 000–25 000, it is suggested that AUP is a dimer.

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