نتایج جستجو برای: thermoresistant allergen
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our aim in this study was to identify and characterize allergic proteins in cooked wolf herring fish. we heated the crude extract alternatively at 50, 60, 70, 80, 90, and 100°c for one hour and results were compared by sodium dodecyl sulfate polyacrylamide gel electrophoresis (sds-page). also, proteins were immunoblotted with fish-sensitive patients’ sera. the major allergenic proteins were ide...
Hyperthermia, either alone or combined with radio-, immuno- or chemotherapy, can control tumor growth, but its effect on metastasis is still controversial. In the present study, we investigated the influence of hyperthermia on the metastatic potential of B16-F10 murine melanoma cells. Incubation of melanoma cells at 43 degrees C for 30 min led to a significant decrease in cell viability. About ...
An endonuclease specific for apurinic sites when double-stranded DNA is used as substrate has been isolated from the thermophilic bacterium, Bacillus stearothermophilus; it is a monomeric protein of about 28,000 daltons, without action on normal DNA strands or on alkylated sites. The enzyme is quite thermoresistant in the presence of other proteins, has an optimal temperature of 60 degrees, nee...
vegetative cell, and the more slowly moving component proved to be the heat-resistant spore catalase. The two catalase-anticatalase arcs crossed each other, showing that the enzymes were antigenically distinct. Figure 1 shows a diagrammatic representation of the results of an analysis of sporulating-cell extract by use of the antigen trench method of Osserman (J. Immunol. 84:93, 1960). An earli...
background: allergy is a clinical disorder affecting humans worldwide. allergenic extracts prepared from natural source materials remain heterogeneous in composition and content, but are regularly used for diagnosis and immunotherapy. recombinant allergens are suitable candidates to use in place of natural allergens; however, the recombinant allergens should be assessed and compared with the na...
Enterococcus avium isolated from Apis mellifera beebread produces a thermoresistant bacteriocin with a strain-dependent inhibitory effect on Listeria and without effect on gram-negative bacteria. The bacteriocin appeared to be a polypeptide of about 6 kDa. Genetic analyses revealed no extrachromosomal material in E. avium.
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