Contribution of structural reversibility to the heat stability of the tropomyosin shrimp allergen
| Autor: | Emiri Sakumichi, Taiko Miyasaki, Takayuki Ishimaru, Fumihiko Saratani, Ken'ichi Hanaoka, Akihito Harada, Hiroyuki Azakami, Chiho Sato-Minami, Masakatsu Usui |
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| Rok vydání: | 2013 |
| Předmět: |
Antigenicity
Circular dichroism Hot Temperature Marsupenaeus Tropomyosin medicine.disease_cause Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Mice Allergen Penaeidae medicine Animals Molecular Biology Chromatography biology Chemistry Protein Stability Organic Chemistry Significant difference Heat stability General Medicine Allergens biology.organism_classification Shrimp Biotechnology |
| Zdroj: | Bioscience, biotechnology, and biochemistry. 77(5) |
| ISSN: | 1347-6947 |
| Popis: | Tropomyosins are common heat-stable crustacean allergens. However, their heat stability and their effects on antigenicity have not been clarified. We purified tropomyosin in this study from raw kuruma prawns (Marsupenaeus japonicus) without heat processing. SDS–PAGE of the purified protein showed a band at approximately 35 kDa that cross-reacted with IgE from the serum of a shrimp-allergic patient, identifying it as Pen j 1. The circular dichroism spectrum of native Pen j 1 revealed the common α-helical structure of tropomyosins which easily collapsed upon heating to 80 °C. However, there were no insoluble aggregates after heating, and the protein regained its native CD spectral pattern after cooling to 25 °C. There was no significant difference in total IgG production between mice sensitized with native and heated Pen j 1. These results suggest that heat-denatured Pen j 1 refolded upon cooling and maintained its antigenicity following the heat treatment. |
| Databáze: | OpenAIRE |
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