Purification and analysis of a human sarcoma associated antigen.
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).
Laboratory of Immunodiagnosis, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
N K
NK
Gupta
Y
Y
Hirshaut
B
B
Schmall
C
C
Feit
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000951:Antigens, Neoplasm / Q000737:chemistry / Q000302:isolation & purification*; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D006801:Humans; D007668:Kidney / Q000276:immunology; D009363:Neoplasm Proteins / Q000737:chemistry / Q000302:isolation & purification*; D012509:Sarcoma / Q000276:immunology*
D000596:Amino Acids; D000951:Antigens, Neoplasm; D009363:Neoplasm Proteins; C081763:sarcoma-associated antigen S1