[Identification and characteristics of concanavalin A-binding neurospecific glycoproteins in human brain and brain tumors].

Soluble and membrane-bound neurospecific Con A-binding glycoproteins from human brain and tumours were identified and characterized, using a procedure which included stepwise extraction with low and high ionic strength buffers, buffered. Triton X-100 and sodium deoxycholate followed by ConA-Sepharose column chromatography, SDS-PAAG electrophoresis and immunoblotting. Adsorbed antisera against different types of neurospecific glycoproteins were used. The bulk of neurospecific glycoproteins (11 and 13) were revealed in protein fractions extracted with low ionic strength buffers and Triton X-100. In astrocytomas and glyoblastomas, some neurospecific glycoproteins were absent. Some glycoproteins were found in tumours, but were absent in brain tissue. Soluble, 77 kD glycoprotein, 11 and 16 kD glycoproteins solubilized with high ionic strength buffers and intrinsic membrane-bound 51, 57, 61, 74 and 77 kD glycoproteins can be viewed as stable neurospecific markers in malignant brain tumours.