Purification, from cultured human choriocarcinoma cells, of a 75000-Mr protein reacting with antibodies to a synthetic peptide based on a cloned human endogenous provirus nucleotide sequence.

Abstract

We previously detected in cultured choriocarcinoma cells a 75000-Mr polypeptide defined by immunoblotting with antibody to a synthetic peptide Sp23 (Cys-Glu-Asn-Pro-Ser-Gln-Phe-Tyr-Glu-Asp-Leu) based on a cloned human endogenous proviral nucleotide sequence. On immunohistological staining, anti-Sp23 stains antigen(s) in the syncytiotrophoblasts of first-trimester placentas and in renal-cell adenocarcinoma tissues. The present report describes purification to homogeneity of the protein from cultured choriocarcinoma cells. The procedure involves extraction with non-ionic detergent and h.p.l.c. using, sequentially, gel-permeation, anion-exchange and reverse-phase columns. The yield was 110 micrograms/g of total choriocarcinoma-cell protein. The results indicate that the purified protein is a monomeric and relatively hydrophilic molecule of Mr 75000.

• Authors: A Närvänen
• Journal: The Biochemical journal (Biochem J) Vol. 231 Issue 1 Pg. 53-7 (Oct 01 1985) ISSN: 0264-6021 [Print] England
• PMID: 3840684 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antibodies
• DNA, Viral
• Neoplasm Proteins
• Oligopeptides
• cysteinyl-glutamyl-asparaginyl-prolyl-serinyl-glutaminyl-phenylalanyl-tyrosyl-glutamyl-aspartyl-leucine

Topics

• Antibodies (immunology)
• Base Sequence
• Cells, Cultured
• Choriocarcinoma (analysis)
• Chromatography, High Pressure Liquid
• DNA, Viral
• Electrophoresis, Polyacrylamide Gel
• Female
• Humans
• Neoplasm Proteins (immunology, isolation & purification)
• Oligopeptides (immunology)
• Pregnancy