Purification of human alpha uterine protein

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Abstract
Human .alpha. uterine protein (AUP) was 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 labeled with 125I by chloramine T. When analyzed by sodium dodecyl sulfate [SDS] gel electrophoresis this radioiodinated protein fraction contained 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 MW estimate of 50,000. Since SDS gel electrophoresis revealed a polypeptide MW of 23,000-25,000, AUP is evidently a dimer.

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