scholarly journals Characterization of Glycoproteins in Pancreatic Cyst Fluid Using a High-Performance Multiple Lectin Affinity Chromatography Platform

2013 ◽  
Vol 13 (1) ◽  
pp. 289-299 ◽  
Author(s):  
Francisca Owusu Gbormittah ◽  
Brian B. Haab ◽  
Katie Partyka ◽  
Carolina Garcia-Ott ◽  
Marina Hancapie ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
High Performance ◽  
Pancreatic Cyst ◽  
Cyst Fluid ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity ◽  
Pancreatic Cyst Fluid

Molecular characterization of the surface and cyst fluid components of Taenia crassiceps

Parasitology ◽  
1990 ◽  
Vol 101 (1) ◽  
pp. 115-125 ◽  
Author(s):  
S. Lamsam ◽  
D. P. McManus
Keyword(s):  
Serum Proteins ◽  
Cyst Fluid ◽  
Surface Proteins ◽  
Lectin Affinity Chromatography ◽  
Taenia Crassiceps ◽  
Tegumental Surface ◽  
Lectin Affinity ◽  
Terminal Galactose ◽  
Sds Page

SUMMARYInformation relating to the characterization of cestode surface macromolecules is limited. This is especially the case with Taenia crassiceps, a well-recognized model for the study of larval cestodiasis. Here, the protein and glycoprotein composition of the tegumental surface and cyst fluid of the metacestode have been investigated using radio-isotope labelling, immunoprecipitation, SDS–PAGE and lectin affinity chromatography. A restricted number of surface proteins was labelled with the 125I/Iodogen method although the majority were immunogenic; in contrast an array of cyst fluid antigens were labelled. Host serum proteins, including immunoglobulins, were identified on the surface and in the cyst fluid. Some of the 125I-labelled surface proteins, including a 37 kDa molecule, have been shown to be glycoproteins and probably contain-D-mannose and/or D-glucose; there is limited or no N-acetylglucosamine and no terminal galactose present on these components. A 37 kDa surface molecule, possibly the same glycoprotein, was also precipitated by infection sera and this may endorse the theory that highly immunogenic carbohydrates are continuously shed by T. crassiceps as a mechanism for diverting the immune response of the host. Radio-iodinated and biosynthetically labelled T. crassiceps antigens were highly cross-reactive with antibody raised to other cestodes and not one antigen was identified as a possible candidate for use in specific immunodiagnosis of any of the important taeniid infections.

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