Parallelism of subcellular location of major particulate neuraminidase and gangliosides in rabbit brain cortex

G. Tettamanti, A. Preti, A. Lombardo, F. Bonali, V. Zambotti

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The subcellular distribution of major particulate neuraminidase and gangliosides in the rabbit cortex was determined. The neuraminidase and gangliosides were found to be present in: (a) the nerve endings; (b) the light membranes of microsomal origin ; (c) the myelin-rich preparation obtained from the crude mitochondrial fraction. Their distribution patterns were very similar also from the quantitative point of view; in fact 40 % of the neuraminidase activity and 43.5 % of the gangliosides were recovered in the nerve endings; 50% of the enzyme and 45% of the gangliosides in the light microsomal membranes; 8 % of the neuraminidase and 11 % of the gangliosides in the myelin-rich preparation. Conversely, the preparations enriched in nuclei, mitochondria and lysosomes were practically devoid of both neuraminidase and gangliosides. The ganglioside patterns of the different subcellular fractions were similar, except for the myelin-rich subfraction which contained higher amounts of monosialoganglioside GM1. The microsomal light membranes had a slightly lower content of trisialoganglioside GTIb and tetrasialoganglioside GQ1 than the nerve endings. These results may be considered consistent with the hypothesis that neuraminidase and gangliosides are fundamental components of the neuronal plasma membrane, thus following the distribution of the different neuronal fragments after homogenization and fractionation.

Original languageEnglish
Pages (from-to)466-477
Number of pages12
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume306
Issue number3
DOIs
Publication statusPublished - Jun 21 1973

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Gangliosides
Neuraminidase
Brain
Rabbits
Nerve Endings
Myelin Sheath
Membranes
Light
Mitochondria
Subcellular Fractions
Cell membranes
Fractionation
Lysosomes
Cell Membrane
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Endocrinology
  • Medicine(all)

Cite this

Parallelism of subcellular location of major particulate neuraminidase and gangliosides in rabbit brain cortex. / Tettamanti, G.; Preti, A.; Lombardo, A.; Bonali, F.; Zambotti, V.

In: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism, Vol. 306, No. 3, 21.06.1973, p. 466-477.

Research output: Contribution to journalArticle

Tettamanti, G. ; Preti, A. ; Lombardo, A. ; Bonali, F. ; Zambotti, V. / Parallelism of subcellular location of major particulate neuraminidase and gangliosides in rabbit brain cortex. In: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism. 1973 ; Vol. 306, No. 3. pp. 466-477.
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