The chemical structure of synaptic membranes

Morgan, Ian G.; Jp, Zanetta; Breckenridge, W. C.; Vincendon, G.; Gombos, G.

doi:10.1016/0006-8993(73)90703-8

Cited by 119 publications

(20 citation statements)

References 40 publications

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“…A number of workers have studied glycoprotein of brain synaptosomal membrane, and bands produced on sodium sulphate-polyacrylamide-gel electrophoresis that could indicate Thy-i were only sometimes found (Banker et al, 1972;Morgan et al, 1973;Zanetta et al, 1975;Waehneldt et al, 1971;Gurd et al, 1974). Given the characterization of Thy-i glycoprotein in the present paper, more definitive experiments should now be possible.…”

Section: Importance Of Thy-i In Rat Brainmentioning

confidence: 98%

Purification of the Thy-1 molecule from rat brain

Barclay

Letarte-Muirhead

Williams

1975

Biochemical Journal

112

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The present paper describes the characterization of the Thy-i molecule from rat brain. The molecule was recognized by its antigens, which could be solubilized from brain membrane with deoxycholate. In the solubilized form the Thy-i antigens were associatQd with a homogeneous component with the following hydrodynamic properties: s2O,W= 2.2S, v = 0.72ml/g and Stokes radius = 3.0nm. The mol.wt. of the deoxycholateantigen complex was estimated to be 27000; these values are not significantly different from those obtained thymocyte Thy-i. Brain Thy-i was further purified by affinity chromatography with lentil lectin coupled to Sepharose 4B, and more than 80 % of the antigen was bound. The material eluted with methyl a-D-glucopyranoside was then filtered on a column of Sephadex G-200, and only one glycoprotein was found in the antigenically active fraction. On sodium dodecyl sulphate-polyacrylamide-gel electrophoresis the glycoprotein was very similar to the Thy-i from thymocytes that binds to lentil lectin. Its apparent mol.wt. on 12.5% acrylamide gels was 24000, and it electrophoresed as a symmetrical band. Brain Thy-l was antigenically indistinguishable from thymocyte Thy-i when analysed with rabbit antisera raised against brain or thymocyte Thy-1.

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Section: Importance Of Thy-i In Rat Brainmentioning

confidence: 98%

Purification of the Thy-1 molecule from rat brain

Barclay

Letarte-Muirhead

Williams

1975

Biochemical Journal

112

View full text Add to dashboard Cite

show abstract

“…Separation of individual glycoproteins by other techniques such as preparative gel electrophoresis can now be envisaged. Moreover, these studies will be extended to the glycoproteins of the synaptosomal plasma membrane in order to investigate our suggestion that the SV and the synaptosomal plasma membrane contain some common glycoproteins [4,6,12].…”

Section: Resultsmentioning

confidence: 99%

“…Highly purified synaptic vesicles were prepared by the method of Morgan et al [2]. Solubilization and affinity chromatography were as previously described [9] .…”

Section: Methodsmentioning

confidence: 99%

“…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.…”

Section: Introductionmentioning

confidence: 99%

“…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] .…”

Section: Introductionmentioning

confidence: 99%

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