Analysis of the glycoforms of Trypanosoma brucei variant surface glycoproteins by MALDI-TOF

2000 ◽  
Vol 28 (3) ◽  
pp. A74-A74
Author(s):  
Angela Mehlert ◽  
Michael A.J. Ferguson
Keyword(s):  
Trypanosoma Brucei ◽  
Maldi Tof ◽  
Variant Surface Glycoproteins ◽  
Surface Glycoproteins

scholarly journals The isolation of plasmids containing dna complementary to messenger rna for variant surface glycoproteins of Trypanosoma brucei

Gene ◽  
1980 ◽  
Vol 8 (4) ◽  
pp. 391-417 ◽  
Author(s):  
J.H.J. Hoeijmakers ◽  
P. Borst ◽  
J. van den Burg ◽  
C. Weissmann ◽  
G.A.M. Cross
Keyword(s):  
Trypanosoma Brucei ◽  
Messenger Rna ◽  
Variant Surface Glycoproteins ◽  
Surface Glycoproteins

Stable Expression of Mosaic Coats of Variant Surface Glycoproteins in Trypanosoma brucei

Science ◽  
1996 ◽  
Vol 272 (5269) ◽  
pp. 1795-1797 ◽  
Author(s):  
J. L. Munoz-Jordan ◽  
K. P. Davies ◽  
G. A. M. Cross
Keyword(s):  
Trypanosoma Brucei ◽  
Stable Expression ◽  
Variant Surface Glycoproteins ◽  
Surface Glycoproteins

Two variant surface glycoproteins of Trypanosoma Brucei of different sequence classes have similar 6 Å resolution X-ray structures

Nature ◽  
1987 ◽  
Vol 325 (6099) ◽  
pp. 84-86 ◽  
Author(s):  
P. Metcalf ◽  
M. Blum ◽  
D. Freymann ◽  
M. Turner ◽  
D. C. Wiley
Keyword(s):  
Trypanosoma Brucei ◽  
X Ray ◽  
Variant Surface Glycoproteins ◽  
Surface Glycoproteins

scholarly journals Selective cleavage of variant surface glycoproteins from Trypanosoma brucei

1979 ◽  
Vol 178 (3) ◽  
pp. 689-697 ◽  
Author(s):  
J G Johnson ◽  
G A Cross
Keyword(s):  
Trypanosoma Brucei ◽  
Large Fragment ◽  
Terminal Fragment ◽  
Large N ◽  
Tryptic Cleavage ◽  
Large Product ◽  
And Function ◽  
Variant Surface Glycoproteins ◽  
Surface Glycoproteins ◽  
Terminal Domains

Two conformationally distinct regions were revealed by tryptic cleavage of six undenatured variant surface glycoproteins purified from clones of Trypanosoma brucei. Within 5 min, the native glycoproteins (65,000 mol.wt.) were cleaved, yielding a large N-terminal fragment (48,000-55,000 mol.wt. depending on the variant) together with one or more C-terminal fragments. After 30-60 min incubation, further breakdown of the large fragment occurred in some variants. The ultimate large product (40,000-52,000 mol.wt.) was very resistant to further degradation by trypsin (in the absence of denaturation). The distinction between N-terminal and C-terminal domains may be significant in relation to the organization and function of these glycoproteins on the trypanosome surface.

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