Allomyrina dichotoma lectin-nonreactive alpha-fetoprotein in hepatocellular carcinoma and other tumors: comparison with Ricinus communis agglutinin-I.

Allomyrina dichotoma lectin (allo A) with a specificity to beta-D-galactose was used to fractionate human alpha-fetoprotein (AFP) by affinity electrophoresis. AFP from cord sera and serum of a patient with fulminant hepatitis showed single bands with a high affinity for allo A. Some patients with hepatocellular carcinoma and patients with gastric cancer and yolk sac tumor had two additional AFP bands, one weakly reactive and the other nonreactive with allo A. Patterns of AFP bands obtained with Ricinus communis agglutinin-I (RCA-I) and erythroagglutinating phytohemagglutinin from Phaseolus vulgaris were entirely different from those obtained with allo A. Of the two common bands reactive with RCA-I, the weakly reactive one was relatively intense in some malignant patients and the strongly reactive one was detected in patients with extrahepatic tumors. Thus, affinity electrophoresis with those lectins provides a potentially useful adjunct for the discrimination between benign and malignant conditions with increased serum levels of AFP.