Concanavalin-A-affinity molecular heterogeneity of human hepatoma AFP and cord-serum AFP.

Glycosylation of alpha-fetoprotein (AFP) by human primary hepatocellular carcinoma (PHC) is abnormal. Concanavalin A (Con A)-affinity molecular variant patterns of serum AFP from patients with PHC are different from those of cord-serum AFP. Different patients with PHC exhibit different Con-A-affinity AFP molecular variant patterns, and the pattern remains constant over time in a given individual. The degree of deviation of the AFP molecular variant pattern from the molecular pattern of AFP secreted by neonatal liver cells is independent of the total serum AFP concentration. We propose that analysis of the AFP lectin-affinity molecular heterogeneity will improve the discrimination between malignant and nonmalignant liver disease in cases when the degree of elevation of the serum AFP concentration is nondiagnostic.