The Purification and Characterization of a Thy-1-like Glycoprotein from Chicken Brain

Overview

Journal Biochem J

Specialty Biochemistry

Date 1983 Jul 1

PMID 6137208

Citations 3

Authors

J A Rostas

T A Shevenan

C M Sinclair

P L Jeffrey

Affiliations

Soon will be listed here.

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.

Citing Articles

The human Thy-1 gene: structure and chromosomal location.

Seki T, Spurr N, Obata F, Goyert S, Goodfellow P, Silver J Proc Natl Acad Sci U S A. 1985; 82(19):6657-61.

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Isolation and characterization of mouse Thy-1 genomic clones.

Chang H, Seki T, Moriuchi T, Silver J Proc Natl Acad Sci U S A. 1985; 82(11):3819-23.

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Neuronal cell adhesion molecules and cytotactin are colocalized at the node of Ranvier.

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