Membrane bound neuraminidase in the brain of different animals: behaviour of the enzyme of endogenous sialo derivatives and rationale for its assay

G. Tettamanti, A. Preti, A. Lombardo, T. Suman, V. Zambotti

Research output: Contribution to journalArticle

Abstract

The activity of brain membrane bound neuraminidase on endogenous and exogenous substrates was comparatively studied in various animals (rat, chicken, rabbit, pig, calf and human). The maximum rate of hydrolysis of endogenous substrates by membrane bound neuraminidase (using a crude preparation of the enzyme) was different in the various animals (from 0.05 to 0.73 units, referred to 1 mg protein) and was obtained under similar but not identical optimum conditions (pH from 4.1 to 5.1; requirement or not of Triton X 100). The maximum degree of hydrolysis of endogenous substrates was also different (from 15 to 27 nmol released NeuNAc/mg protein) and was obtained within different incubation periods (from 2 to 18 hr). It corresponded (in rabbit, calf, human brain only), or not, to the actual exhaustion of the endogenous substrates. The endogenous substrates were recognized as both gangliosides and sialoglycoproteins. The extent of hydrolysis of sialoglycoproteins varied from 1.5% in rabbit to 15.6% in chicken brain; the hydrolysis of gangliosides (ranging from 14.1% in pig to 53.7% in rabbit brain) reached only in some animals (rabbit, calf, human) the complete transformation of major oligosialogangliosides into the neuraminidase resistant monosialoganglioside GMI. Upon addition of exogenous substrates (sialyl lactose, ganglioside GD1a, brain sialopeptides, ovine submaxillary mucin) the actual rate of liberation of total NeuNAc (from both endogenous and exogenous substrates) considerably exceeded, although to a different extent (depending on the animal and on the added substrate used) the rate of hydrolysis of sole endogenous substrates. The possibility of an accurate assay of brain membrane bound neuraminidase in a crude enzyme preparation is evaluated and guidelines for the assay procedure suggested.

Original languageEnglish
Pages (from-to)451-456
Number of pages6
JournalJournal of Neurochemistry
Volume25
Issue number4
DOIs
Publication statusPublished - 1975

Fingerprint

Animal Behavior
Neuraminidase
Assays
Brain
Animals
Derivatives
Membranes
Hydrolysis
Rabbits
Substrates
Enzymes
Sialoglycoproteins
Gangliosides
Chickens
Swine
Octoxynol
Mucins
Sheep
Proteins
Guidelines

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Membrane bound neuraminidase in the brain of different animals : behaviour of the enzyme of endogenous sialo derivatives and rationale for its assay. / Tettamanti, G.; Preti, A.; Lombardo, A.; Suman, T.; Zambotti, V.

In: Journal of Neurochemistry, Vol. 25, No. 4, 1975, p. 451-456.

Research output: Contribution to journalArticle

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