[A study of membrane glycoproteins from the rat brain using D-galactose-specific lectin].
Immobilized D-galactose-specific lectin from Zea mais was used to purify rat brain membrane glycoproteins. The membrane glycoproteins preliminarily washed from soluble proteins were solubilized consecutively by 2% triton X-100 and 1% SDS. PAG-electrophoresis with SDS and 2-mercaptoethanol revealed 10 polypeptide bands (Mm 109, 62, 59, 54, 51, 42, 16, 14, 12.5 and 12 kDa) in the membrane fraction of glycoproteins solubilized with triton X-100. Additional solubilization with SDS revealed 3 bands (Mm 109, 62, and 54 kDa). Only 3 polypeptide bands (Mm 62, 59, 42 kDa) were identified when analogous procedure was used for purification of the rat liver glycoproteins. Horse radish peroxidase labelled D-galactose-specific lectin from Zea mais was found to bind to neuron bodies and neurites in the cerebellum. It is suggested that the identified brain-specific membrane glycoproteins may take part in the cell adhesion between neurons.
Berezin
V A
VA
Rudenko
O A
OA
Boĭko
I I
II
Gaĭdar
Iu A
IuA
Lepekhin
E A
EA
D000818:Animals; D001923:Brain Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005690:Galactose; D037102:Lectins; D008562:Membrane Glycoproteins / Q000032:analysis*; D010455:Peptides / Q000032:analysis; D051381:Rats
D037102:Lectins; D008562:Membrane Glycoproteins; D010455:Peptides; D005690:Galactose
Izuchenie membrannykh glikoproteinov mozga krysy s ispol'zovaniem D-galaktozospetsificheskogo lektina.