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Purification and analysis of a human sarcoma associated antigen
N K Gupta1, Y Hirshaut, B Schmall
1Laboratory of Immunodiagnosis, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
Cancer Letters
|May 14, 1993
Summary
Researchers purified the S1 heterophile antigen found on human sarcoma cells. This protein, present in guinea-pig kidney, was characterized as a 70,000 Da monomer with a specific amino acid sequence.
Area of Science:
- Biochemistry
- Immunology
- Cell Biology
Background:
- S1 is a heterophile antigen identified on human sarcoma cell lines.
- The antigen's presence has also been noted in guinea-pig kidney tissue.
Purpose of the Study:
- To achieve homogeneous purification of the S1 antigen.
- To characterize the biochemical properties of the purified S1 antigen.
Main Methods:
- Purification involved ammonium sulfate fractionation, DEAE-cellulose, sephadex, high-pressure liquid chromatography, and affinity chromatography.
- Protein molecular weight was determined by SDS-PAGE.
- Amino acid composition and N-terminal sequencing were performed.
Main Results:
- The S1 antigen was successfully purified to homogeneity.
- SDS-PAGE revealed S1 as a monomeric protein with a molecular weight of 70,000 Da.
- Amino acid analysis indicated a prevalence of glycine, lysine, and glutamic acid, with aspartic acid as the N-terminal residue followed by glycine-valine-alanine-glutamic acid.
Conclusions:
- The S1 antigen is a well-defined 70 kDa monomeric protein.
- The N-terminal amino acid sequence provides a basis for further structural and functional studies of the S1 antigen.
