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Affinity chromatography on Con A‐Sepharose of synaptic vesicle membrane glycoproteins
Author(s) -
Zanetta J.P.,
Gombos G.
Publication year - 1974
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(74)81029-x
Subject(s) - citation , chemistry , combinatorics , library science , computer science , mathematics
Dekirmenjian and Brunngraber [l] have reported that adult rat brain synaptic vesicles do not contain protein-bound sialic acid. However our previous studies on highly purified synaptic vesicles (SV) [2] have shown that they contain high levels of proteinbound carbohydrate [3-51 which cannot be explained by the synaptosomal plasma membrane (SPM) contamination of less than 10% determined by chemical and enzymatic markers [2] . In addition, the molar compositions of protein-bound sugars of SV and SPM are too different [4] for the SV sugars to be explained by SPM contamination. Moreover, the electrophoretic profiles of SV are significantly simpler than those of the SPM [6,7] which is not the case with SV contaminated with SMP [8] . As a first step towards detailed studies of the SV glycoproteins, we have attempted to separate them by affinity chromatography on Sepharose-bound Concanavalin A (Con A-Sepharose) in the presence of sodium dodecyl sulphate (SDS).