IMMUNOCHEMICAL STUDIES OF ISOLATED HUMAN BRAIN GANGLIOSIDE COMPONENTS

Abstract— Gangliosides G1 to G5 were isolated from human brain by means of TLC and tested with respect to their specificity to antisera against normal brain and Tay‐Sachs brain gangliosides by agar double diffusion analysis. Gangliosides G2 and G4 gave precipitation reactions with antisera to normal human gangliosides (NHG) while only ganglioside G6 reacted with antisera to Tay‐Sachs gangliosides (TSG). Additional specificity information was also obtained by use of the enzyme neuraminidase for the removal of specific sialic acid (NANA) residues. It was concluded from these data that the specificity of the anti‐NHG antibodies is determined by the presence of a galactose (β1, 3) N‐acetyl galactos‐amine–while that of anti‐TSG antibodies is due to a N‐acetyl galactosamine (β1, 4) galactose‐end sequence. By means of natural compounds of known structure it was found that both the sequence of carbohydrate residues and position of NANA residues in the molecule played a critical role in the formation of precipitation bands with NHG‐antisera. This information was utilized to distinguish one isomeric form of disialoganglioside from another, i.e. G2 from G3 and to confirm the structure of the trisialoganglioside, G1. The immunochemical method appears to be a useful one for elucidating structural differences in ganglioside molecules. Copyright © 1969, Wiley Blackwell. All rights reserved