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. 1983 Jul 1;213(1):143–152. doi: 10.1042/bj2130143

The purification and characterization of a Thy-1-like glycoprotein from chicken brain.

J A Rostas, T A Shevenan, C M Sinclair, P L Jeffrey
PMCID: PMC1152101  PMID: 6137208

Abstract

We have purified from chicken forebrain a membrane glycoprotein that is enriched in purified synaptic membranes and has an apparent mol.wt. of 22 800 in 15% sodium dodecyl sulphate/polyacrylamide gels. This molecule was compared with rat and human brain Thy-1 glycoproteins purified by the same procedure in order to determine whether it could be a homologue of Thy-1. Although polyvalent heterologous antisera raised against the rat and chicken molecules showed no immunological cross-reactivity with the other glycoprotein, a great deal of physical and chemical similarity was demonstrated between the chicken glycoprotein and rat Thy-1. Their apparent molecular weights, subcellular localization and amino acid and amino sugar compositions are very similar. C.d. spectra show that both molecules contain predominantly a beta-sheet and structure with no detectable alpha-helix. Electrophoretic analysis of the CNBr-cleaved molecules under reducing and non-reducing conditions shows that both molecules contain intramolecular disulphide bridges. Taken together these results suggest that the chicken brain glycoprotein is an immunologically distinct homologue of the mammalian Thy-1 glycoproteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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