Abstract:
:The endogenous sialidase (N-acetylneuraminidase) activity of membranes prepared from goldfish retina and optic tectum displays characteristics similar to those reported for neural plasma membrane sialidases of other organisms. Endogenous membrane sialidase activity was found to be optimal at ph 4.0, and maximal release was obtained at 37-50 degrees C, above which temperature thermal instability of the preparations was observed. Optic nerve crush, which results in regeneration of retinal ganglion cell axons, did not result in significant changes in measured endogenous membrane sialidase activity in either the retina or the optic tectum. Enzymatic hydrolysis of membrane sialoglycolipid (ganglioside) accounted for about 70% of the total sialic acid released. Ganglioside GM1 accumulated as the major lipid product in both retina and tectum, indicating that the inner sialosylgalactosyl linkage in the ganglio oligosaccharide series was resistant to hydrolysis by the endogenous enzyme.
journal_name
Neurochem Resjournal_title
Neurochemical researchauthors
Leskawa KC,Agranoff BWdoi
10.1007/BF00965657subject
Has Abstractpub_date
1983-01-01 00:00:00pages
99-112issue
1eissn
0364-3190issn
1573-6903journal_volume
8pub_type
杂志文章abstract::In membranes of rat striatum, phorbol 12-myristate 13-acetate (PMA), a potent activator of Ca2+/phospholipid-dependent protein kinase, enhanced adenylate cyclase activity by counteracting the inhibition elicited by GTP. Exposure to pertussis toxin caused a similar alteration of the GTP-regulation of the enzyme activit...
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