Glycoprotein pattern in human brain tumors studied using lectin binding after sodium dodecyl sulfate-gel electrophoresis and protein blotting.

The immunoblotting technique was used to study the glycoproteins in human brain tumor samples including astrocytoma, glioblastoma, meningioma and oligodendroglioma, as well as in normal human brain. Glycoproteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, electrophoretically transferred to nitrocellulose membrane and characterized, using binding with 11 different lectins. Tumor-associated glycoproteins were found using the lectins peanut agglutinin (PNA), soybean agglutinin, Limulus polyhemus, Lotus tetragonolobus, Ricinus communis 1, (RCA-1) and wheat germ agglutinin (WGA). Their molecular masses ranged from 50 to 180 kDa. Several of them were common to the 3 types of tumors: astrocytomas, oligodendrogliomas and meningiomas. PNA, RCA-1 and WGA were the 3 most feasible lectins with regard to tumor specificity, simplicity and reproducibility.