Purification and analysis of a human sarcoma associated antigen Journal Article


Authors: Gupta, N. K.; Hirshaut, Y.; Schmall, B.; Feit, C.
Article Title: Purification and analysis of a human sarcoma associated antigen
Abstract: S1, a heterophile antigen present on human sarcoma cell lines in culture, has been previously defined by this laboratory [1,2]. This antigen is also present in guinea-pig kidney. Purification of the antigen to homogeneity has now been achieved by a combination of ammonium sulfate fractionation, DEAE-cellulose, sephadex, high pressure liquid chromotography and affinity chromotography. S1 is a monomeric protein of 70 000 Da, as indicated by the presence of a single band on SDS-PAGE. Amino acid analysis demonstrates the prevalence of glycine, lysine and glutamic acid. Aspartic acid was found to be the N-terminal residue with further sequence of glycine-valine-alanine-glutamic acid (gly-val-ala-glut). © 1993.
Keywords: human cell; nonhuman; animal; animal tissue; neoplasm proteins; tumor antigen; animalia; sarcoma; kidney; antigen; amino terminal sequence; antigens, neoplasm; tumor cell line; amino acids; glutamic acid; molecular weight; aspartic acid; lysine; glycine; polyacrylamide gel electrophoresis; electrophoresis, polyacrylamide gel; amino acid analysis; purification; guinea pig; guinea pigs; antigen purification; human; priority journal; article; sus scrofa; cavia porcellus; sarcoma antigen; electrophoresis, disc
Journal Title: Cancer Letters
Volume: 69
Issue: 3
ISSN: 0304-3835
Publisher: Elsevier Ireland Ltd.  
Date Published: 1993-05-14
Start Page: 173
End Page: 180
Language: English
DOI: 10.1016/0304-3835(93)90171-5
PUBMED: 8513443
PROVIDER: scopus
DOI/URL:
Notes: Source: Scopus
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