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Background: Buckwheat is a common dish in Japan, Korea, and other countries. The buckwheat allergen, a 16-kDa protein, was previously described as a pepsin-resistant protein linked to immediate-type allergies to buckwheat. However, it is unknown if recombinant BWp16 will react with a patient's IgE is uncertain. Methods: Based on the sequences obtained by the 521-rapid amplification of cDNA ends and 3U2032-RACE PCR, the cDNA encoding BWp16 from Japanese buckwheat seeds was cloned. Using affinity chromatography, a Recombinant BWp16 protein isolated in Escherichia coli was purified. BWp16 purified recombinant BWp16 serum, coagulation, and cross inhibition tests were performed using sera from patients with positive IgE binding to buckwheat and controls. Patients with positive IgE binding to buckwheat reacted with the purified BWp16. This refined recombinant BWp16 can be used in the diagnosis of buckwheat allergy.
Source link: https://doi.org/10.1159/000092038
Background: Exposure to the house dust mite Blomia tropicalis is increasingly being attributed to asthma exacerbation in sensitized people. Methods: A u03bbgt22A cDNA library was constructed from B. tropicalis mRNA and tested using specific DNA probes. paraphrase protease preproenzyme from B. tropicalis that was discovered by sequencing analysis. BLAST analysis of the deduced amino acid sequence revealed high homology between clone Bt2-3 and serine proteases from domestic dust mites, showing high homology. paraphrase proteases' serine active site and the histidine active site of serine proteases were both preserved. The serine protease active sites are highly preserved among the clinically important mite species, including B. tropicalis. Conclusion: We present the cloning and molecular characterization of a B. tropicalis cDNA clone encoded a trypsin-like protease with a potential role as an allergen.
Source link: https://doi.org/10.1159/000068375
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