Abstract
A glycoprotein associated with malignancy was purified from the 0.6 m perchloric acid-soluble fraction of serum obtained from cancer patients. The purified glycoprotein contained sialic acid, which was reponsible for binding to wheat-germ agglutinin-Sepharose. Gel electrophoresis showed one band with an apparent M r of 50 000–55 000, and the isoelectric point was 4.4±0.1. The glycoprotein could be distinguished from carcinoembryonic antigen and α-fetoprotein. Iodination of this material with chloramine-T permitted development of a radioimmunoassay.
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