Distinct glycosylation of serum proteins in patients with cancer: brief communication

Concanavalin A and wheat germ agglutinin, lectins that interact with serum glycoprotein in a manner similar to the antigen--antibody reaction, were used as "antibodies" in a single radial immunodiffusion technique to test a coded serum panel (from the National Cancer Institute, Bethesda, Md., and the Mayo Clinic, Rochester, Minn.) containing a) 99 serum samples from patients with different types of malignant neoplasms of the gastrointestinal tract, prostate gland, and lung, b) 50 samples from patients with benign diseases of the same organs as those affected in the cancer patients, and c) 50 samples from apparently healthy smokers. The resulting precipitation rings were not correlated to serum protein concentration, and the differences (demonstrated by Student's t-test and with a generalization of the one-sided two-sample Kolmogorov-Smirnov statistic for evaluating diagnostic tests) established that serum glycoproteins are glycosylated differently in cancer patients than in people without cancer.