Modified ELISA for hydatid serodiagnosis: the potential of periodate treatment and phosphorylcholine inhibition

1997 ◽  
Vol 8 (3-4) ◽  
pp. 145-148 ◽  
Author(s):  
Silvia Sterla ◽  
Inger Ljungström ◽  
Alberto Nieto
Keyword(s):  
2017 ◽  
Vol 5 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Premalatha Shetty ◽  
Avila D’Souza ◽  
Geethu CP

Peroxidase tagged proteins are being used successfully as immune-histological probes for the demonstration of tissue antigens, and in enzyme amplified immunoassay systems for the quantitative determination of soluble and insoluble antigens. The glycoprotein nature of peroxidases can be exploited for conjugation to proteins of interest. Peroxidase extracted from the bulbs of Brassica oleracea gongylodes was salted out at 40-80% ammonium sulfate saturation and activated by treatment with 1-Fluoro-2,4-dinitro benzene (FDNB) and periodate. Treatment with 0.08% FDNB and 12.5mM periodate was optimized for activation of the enzyme. The treated enzyme was found to conjugate successfully to immunoglobulin fractions harvested from egg yolk (IgY), human plasma and goat serum. Enzyme conjugated to IgY fraction showed improvement in its pH stability and temperature stability. The affinity of the enzyme for its substrate phenol did not alter to a significant extent upon activation and conjugation. The conjugates exhibited high affinity towards phenol, bromocresol purple and bromothymol blue in comparison to HRP conjugates prepared using the same protocol. Int. J. Appl. Sci. Biotechnol. Vol 5(1): 59-65


1976 ◽  
Vol 143 (5) ◽  
pp. 1265-1270 ◽  
Author(s):  
P W Kincade ◽  
P Ralph ◽  
M A Moore

A substance which was mitogenic for murine B lymphocytes in the presence of 2-mercaptoethanol was isolated from agar. Stimulating activity of this material was stable to proteolysis or protein denaturants but was destroyed by periodate treatment. Agar-derived mitogen stimulation was distinct from that obtained with dextran sulfate or lipopolysaccharide and may define different populations of B lymphocytes.


Parasitology ◽  
1999 ◽  
Vol 119 (5) ◽  
pp. 491-501 ◽  
Author(s):  
A. JOACHIM ◽  
B. RUTTKOWSKI ◽  
A. DAUGSCHIES

Living and fixed specimen of Oesophagostomum dentatum were labelled in situ with serum antibodies or a panel of biotin- labelled lectins. Specific binding of antibodies was observed in all parasitic stages – freshly exsheathed 3rd-stage larvae (L3), 3rd- and 4th-stage (L4) larvae cultured in vitro and L3 and L4 and adults isolated from pig intestines. The shedding of the stained layer by motile larvae was inhibited by levamisole-induced paralysis. Larvae cultured in vitro exposed serum-derived proteins on their surface which could be labelled with secondary antibody directed against the respective serum donor species. While freshly exsheathed larvae were recognized by O. dentatum-positive serum only, older larvae and adults cross-reacted with serum from pigs infected with O. quadrispinulatum, a closely related species. Lectin binding varied considerably between stages. While binding was not observed in pre-parasitic stages, Concanavalin A, Soybean Agglutinin, Wheat Germ Agglutinin, Ricinus communis Agglutinin and Peanut Agglutinin bound to developing larvae in varying degrees. Dolichos biflorus Agglutinin only bound to advanced (luminal) larval stages, while adults generally displayed only weak or partial lectin binding (except with Concanavalin A and Wheat Germ Agglutinin). Ulex europaeus Agglutinin only labelled larvae derived from cultures containing 10% pig serum. Cleavage of the carbohydrate residues by sodium periodate treatment resulted in reduction of antibody binding to cultured larvae, but not to freshly exsheathed L3. Concanavalin A, Soybean Agglutinin, and Peanut Agglutinin binding was also reduced by periodate treatment, while binding of Wheat Germ Agglutinin and Ricinus communis Agglutinin was inhibited only in early L3, but not in older stages. The different lectin labelling patterns are related to the different stages of the nematode – infective, invasive, histotropic, and luminal – and may serve as a mode of adaptation for the parasite against the host's immune attack by surface glycoprotein variation, together with antigen shedding (as demonstrated by labelling of motile larvae) and a possible acquisition of host molecules at the parasite's surface. Furthermore, a possible role of this developmental variation in surface carbohydrates in parasite–parasite interactions is discussed.


Allergy ◽  
1997 ◽  
Vol 52 (5) ◽  
pp. 565-569 ◽  
Author(s):  
I. Moneo ◽  
M. T. Audicana ◽  
E. Alday ◽  
G. Curiel ◽  
M. D. Pozo ◽  
...  

1960 ◽  
Vol 15 (9) ◽  
pp. 575-577 ◽  
Author(s):  
E. Mohr

Neuraminidase of Vibrio cholerae is inhibited by N-acetyl-neuraminic acid, but not by methoxyneuraminic acid, the methylester of neuraminic acid, and the degradation product obtained by periodate treatment. Sulfhydryl reagents showed no significant inhibition.


1998 ◽  
Vol 101 (1) ◽  
pp. 67-74 ◽  
Author(s):  
Agnes Bugajska-Schretter ◽  
Lena Elfman ◽  
Thomas Fuchs ◽  
Sonja Kapiotis ◽  
Helmut Rumpold ◽  
...  

1977 ◽  
Vol 82 (2) ◽  
pp. 591-595 ◽  
Author(s):  
Eric C. Reynolds ◽  
Lloyd R. Finch

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