Abstract
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.
Published Version
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