[The problem of structural heterogeneity of brain prealbumin].

The investigation of structural heterogeneity of rat brain prealbumine (BTB-protein) has been carried out. BTB-protein migrates in disc electrophoresis in 7.5% and 10% polyacrylamide gel with the "witness" front of bromthemol blue (BTB). The protein dissociated in three components in 8M urea. Three components with the molecular weight 14500, 8000 and 6900 daltones were found by disc electrophoresis of BTB-protein in 0.1% SDS-Na. Glycine was shown to be N-terminal amino acid of this BTB-protein complex.