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Purification of human alpha uterine protein.

Authors
  • Sutcliffe, R G
  • Bolton, A E
  • Sharp, F
  • Nicholson, L V
  • MacKinnon, R
Type
Published Article
Journal
Journal of reproduction and fertility
Publication Date
Mar 01, 1980
Volume
58
Issue
2
Pages
435–442
Identifiers
PMID: 7431275
Source
Medline
License
Unknown

Abstract

Human alpha uterine protein (AUP) has been prepared from extracts of decudua 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-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 50000. Since SDS gel electrophoresis revealed a polypeptide molecular weight of 23000-25000, it is suggested that AUP is a dimer.

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