scholarly journals Haptoglobin phenotypes and susceptibility of Schistosoma parasites infection in central Sudan

2017 ◽  
Vol 9 (1) ◽  
pp. e2017042 ◽  
Author(s):  
Ashraf Siddig Yousif ◽  
Atif Abdelrahman Elagib

Haptoglobin (Hp) is an acute phase protein that binds the free haemoglobin (Hb), thus preventing iron loss and renal damage. Hp also has anti-oxidative and immunomodulatory properties. Three Hp phenotypes have been identified in human: Hp1-1, Hp2-1 and Hp2-2. Hp polymorphisms have been related to susceptibility of various diseases. In this study we aimed to assess the possible association of Hp phenotypes polymorphism to Schistosoma parasites infection in central Sudan. We have investigated the Hp phenotypes polymorphism distribution in the serum of 125 (93 S. mansonai, 13 S. haematobium and 19 infected with both ‘’co-infection’’) parasitologically confirmed infected individuals and 208 healthy individuals served as control. Hp phenotypes have been determined by polyacrylamide gel electrophoresis followed by benzidine staining. Our study revealed that Hp1-1 percentage frequency was significantly higher in infected individuals than healthy control individuals 51% and 26% respectively. Our data suggest that Hp1-1 phenotype may upsurge the susceptibility to Schistosoma parasites infection in central Sudan.

1998 ◽  
Vol 66 (2) ◽  
pp. 756-759 ◽  
Author(s):  
Disney M. Rosales-Borjas ◽  
Juan Díaz-Rivadeneyra ◽  
Antonio Doña-Leyva ◽  
Sergio A. Zambrano-Villa ◽  
Carmen Mascaró ◽  
...  

ABSTRACT The secretory immune response in humans infected with Giardia lamblia was studied by using saliva samples and a membrane-rich protein fraction. The membrane fraction, studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, showed 24 antigen bands, ranging from 170 to 14 kDa. Saliva samples from giardiasis patients showed a heterogeneous response against the membrane fraction when they were assayed by immunoblotting. Among the antigens recognized by patient saliva samples, those of 170, 105, 92, 66, 32, 29, and 14 kDa stood out. These antigens were not recognized by saliva samples from healthy individuals. They may be of importance in future studies of protection from or diagnosis of G. lamblia infections.


2003 ◽  
Vol 10 (3) ◽  
pp. 383-387 ◽  
Author(s):  
Masahiro Yoneda ◽  
Takao Hirofuji ◽  
Noriko Motooka ◽  
Koji Nozoe ◽  
Kayoko Shigenaga ◽  
...  

ABSTRACT Bacteroides forsythus is one of the important periodontopathic bacteria, and this microorganism is known to have an S-layer outside the outer membrane. The S-layer-like antigens were recently isolated from B. forsythus, and they were found to be 270- and 230-kDa proteins in the envelope fraction. In this study, these proteins were confirmed to be specific to B. forsythus by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and they were clearly recognized by sera from patients with adult and early-onset periodontitis in Western immmunoblot analysis. We compared the immunoglobulin G (IgG) responses against the purified S-layer-like antigen by enzyme-linked immunosorbent assay. IgG responses against this antigen were low in healthy control subjects, but they were significantly higher in subjects with adult and early-onset periodontitis. Together with the fact that the IgG responses against the crude extract of B. forsythus did not rise significantly in patients with periodontitis, S-layer-like proteins are considered to be specific antigens of B. forsythus and may play an important role in the progression of periodontitis.


2012 ◽  
Vol 22 (5) ◽  
pp. 879-883
Author(s):  
Elizabeth Moreira dos Santos Schmidt ◽  
Rogério Ribas Lange ◽  
Érika Fruhvald ◽  
Ivan Felismino Charas do Santos ◽  
José Jurandir Fagliari

Author(s):  
G. L. Brown

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).


Hepatology ◽  
2009 ◽  
pp. NA-NA
Author(s):  
Ieva Peredniene ◽  
Eddy van de Leur ◽  
Birgit Lahme ◽  
Monika Siluschek ◽  
Axel M. Gressner ◽  
...  

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