scholarly journals Glycopeptides derived from individual membrane glycoproteins from control and Rous sarcoma virus-transformed hamster fibroblasts.

1978 ◽  
Vol 253 (17) ◽  
pp. 6092-6099
Author(s):  
G.P. Tuszynski ◽  
S.R. Baker ◽  
J.P. Fuhrer ◽  
C.A. Buck ◽  
L. Warren
1983 ◽  
Vol 209 (3) ◽  
pp. 659-667 ◽  
Author(s):  
L A Hunt

The asparagine-linked oligosaccharides of the complex acidic-type from [3H]mannose-, [3H]glucosamine- or [3H]galactose-labelled membrane glycoproteins of BHK21 cells and Rous-sarcoma virus were analysed by gel filtration combined with extensive digestion with endo- and exo-glycosidases from bacterial and eukaryotic sources. The neutral products from the digestion with a mixture of exoglycosidases and endo-beta-N-acetylglucosaminidase D from Diplococcus pneumoniae included a series of [3H]mannose- and [3H]glucosamine-labelled neutral oligosaccharides that were all converted by digestion with eukaryotic beta-N-acetylglucosaminidases into free N-acetylglucosamine and a small oligomannosyl core containing two alpha-linked mannose residues and a third mannose residue beta-linked to N-acetylglucosamine. These studies suggested that the complex acidic-type oligosaccharides from cellular and viral membrane glycoproteins contained a common oligomannosyl core region (Man2 alpha leads to Man beta leads to GlcNAc2), with heterogeneity in the number and/or linkage of outer branch N-acetylglucosamine residues resulting in partial resistance to beta-N-acetylglucosaminidase from a bacterial source.


1984 ◽  
Vol 49 (2) ◽  
pp. 325-332 ◽  
Author(s):  
F Poirier ◽  
P Jullien ◽  
P Dezelee ◽  
G Dambrine ◽  
E Esnault ◽  
...  

1985 ◽  
Vol 260 (26) ◽  
pp. 14292-14296 ◽  
Author(s):  
S Schuh ◽  
W Yonemoto ◽  
J Brugge ◽  
V J Bauer ◽  
R M Riehl ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document