Further studies on a human lung tumor-associated antigen. Comparison of antigens from different tumors.
A human lung tumor-associated antigen was purified to homogeneity from a crude cell-free extract of a human lung adenocarcinoma using standard biochemical procedures. In order to facilitate monitoring the recovery of antigen, trace amounts of previously purified and radioiodinated antigen from another lung tumor were added to the crude extract. The purified antigen was a glycoprotein and contained sialic acid. The antigen had a molecular weight of 76,000 and appeared to contain three subunits, each with a molecular weight of 25,000. The antigen had the following physical properties: Stokes radius, 39.4 A; S20,w, 4.24 S; D20,w, 5.15 x 10(-7) cm2 S-1; and a frictional ratio of 1.40. In addition, the purified, radioiodinated antigen retained complete immune reactivity since it could be quantitatively precipitated with specific immune serum. All of these properties were in close agreement with the properties of another antigen which was purified from a separate human lung tumor. Thus, it appeared from the biochemical and immunochemical criteria presented in this report that a common and identical antigen was isolated from two distinct human lung tumor extracts.
D000230:Adenocarcinoma / Q000032:analysis* / Q000276:immunology; D000951:Antigens, Neoplasm / Q000276:immunology / Q000302:isolation & purification*; D002474:Cell-Free System; D002846:Chromatography, Affinity; D006023:Glycoproteins / Q000302:isolation & purification*; D006801:Humans; D008175:Lung Neoplasms / Q000032:analysis* / Q000276:immunology; D008970:Molecular Weight; D009362:Neoplasm Metastasis; D012794:Sialic Acids / Q000032:analysis
D000951:Antigens, Neoplasm; D006023:Glycoproteins; D012794:Sialic Acids