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  Further studies on the gangliosidic nature of the cholinergic-specific antigen, Chol-1.

Giuliani, A., Calappi, E., Borroni, E., Whittaker, V. P., Sonnino, S., & Tettamanti, G. (1990). Further studies on the gangliosidic nature of the cholinergic-specific antigen, Chol-1. Archives of Biochemistry and Biophysics, 280(1), 211-216.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-0D86-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-37F1-F
Genre: Journal Article

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Giuliani, A., Author
Calappi, E., Author
Borroni, E.1, Author              
Whittaker, V. P.1, Author              
Sonnino, S., Author
Tettamanti, G., Author
Affiliations:
1Abteilung Neurochemie, MPI for biophysical chemistry, Max Planck Society, ou_578555              

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 Abstract: The antigen designated as Chol-1 beta, detected by an antiserum specific for cholinergic neurons, has been purified to homogeneity from ganglioside mixtures extracted from Torpedo electric organ and pig brain. The final products from the two sources behaved identically in a wide range of tests and gave coincident immunopositive and Ehrlich-positive spots after thin layer chromatography in seven different solvent systems; they were thus considered to be identical and to constitute a single, pure chemical species. Gas-chromatographic analysis revealed the presence of long-chain bases, glucose, galactose, N-acetylgalactosamine, and sialic acid in integral molar ratios of 1:1:2:1:3; the compound's reactivity to cholera toxin after Vibrio cholerae sialidase treatment on thin layer chromatography and the recovery of GM1 as sole product of exhaustive sialidase treatment identified it as a member of the gangliotetrahexosyl series. From the products of partial enzymatic desialylation and treatment with beta-galactosidase and a comparison of the compound's immunoreactivity to anti-Chol-1 antisera with that of other trisialogangliosides of defined molecular structure, we were able to assign a disialosyl residue alpha-Neu5Ac-(2----8)-alpha-Neu5Ac-(2----3)- to the inner galactose, and we suggest GalNAc as a possible site of linkage of the third sialic acid.

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Language(s): eng - English
 Dates: 1990-07
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: eDoc: 285361
ISI: A1990DK20300029
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Title: Archives of Biochemistry and Biophysics
Source Genre: Journal
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Pages: - Volume / Issue: 280 (1) Sequence Number: - Start / End Page: 211 - 216 Identifier: ISSN: 0003-9861