Ganglioside sialidase activity in bovine neuronal perikarya

• Published in: Neurochemical research Vol. 1; no. 2; p. 171
• Main Authors: Schengrund, C L, Nelson, J T
• Format: Journal Article
• Language: English
• Published: United States 01.04.1976
• ISSN: 0364-3190
• DOI: 10.1007/BF00966108

Neuronal perikarya were isolated, using bulk preparative procedures, from bovine brains. Synaptosomes, neuronal perikarya, and brain homogenates had similar ganglioside patterns, with the synaptosomes containing at least four times more total ganglioside per mg protein than the neuronal perikarya and twice that of the homogenate. Synaptosomes had 26-33 nmol total sialic acid/mg protein, while the neurons had only 15-17 nmol. Determination of ganglioside sialidase activity showed that neuronal perikarya had very low levels (negligible), in comparison with synaptosomes or whole-brain homogenates. Trypsin treatment during the isolation procedure enhanced sialidase activity two-to threefold in the particulate fraction of the whole-brain homogenate. Determination of the distribution of sialidase activity in the fractions obtained during the isolation of the neuronal perikarya showed that the sialidase activity was associated with the myelin, broken-off dendritic processes, and glial-cell fractions that banded in the less dense sucrose.