Ganglioside sialidase activity in bovine neuronal perikarya

Cara Lynne Schengrund, Joseph T. Nelson

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)171-180
Number of pages10
JournalNeurochemical Research
Volume1
Issue number2
DOIs
StatePublished - Apr 1 1976

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cellular and Molecular Neuroscience

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