Partial purification and characterization of CA19-9 antigen from the ascitic fluid of a patient with pancreatic cancer.

CA19-9 immunoreactive protein was partially purified from the ascitic fluid of a patient with pancreatic cancer by perchloric acid fractionation, gel chromatography and Affi-gel Blue column chromatography, resulting in a purified sample of 5.0 x 10(6) CA19-9 units per milligram of protein (3700-fold purification). Western blotting analysis of this purified sample revealed a single band of molecular weight 210 kDa. Although the original ascitic fluid showed a high CA125 immunoreactivity, this purified sample had no CA125 immunoreactivity. The elution pattern for CA19-9 activity on Affi-gel Blue column is quite distinct from that for CA125. These results suggest that CA19-9 antigen in carcinoma patients may be identical or very similar to that recently purified from the culture media of the colorectal cell line SW1116 and is distinct from CA125 antigen.