Immunochemical analysis of pepsin-digested fish tropomyosin
A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical pr...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Keshavarz, Behnam [verfasserIn] |
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
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Enthalten in: Defining Tumour Shape Irregularity for Preoperative Risk Stratification of Clinically Localised Renal Cell Carcinoma - Tanaka, Hajime ELSEVIER, 2022, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:118 ; year:2020 ; pages:0 |
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| DOI / URN: |
10.1016/j.foodcont.2020.107427 |
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| 245 | 1 | 0 | |a Immunochemical analysis of pepsin-digested fish tropomyosin |
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| 520 | |a A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. | ||
| 520 | |a A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. | ||
| 650 | 7 | |a Tropomyosin |2 Elsevier | |
| 650 | 7 | |a Pepsin digestion |2 Elsevier | |
| 650 | 7 | |a Epitope mapping |2 Elsevier | |
| 650 | 7 | |a Fish allergen |2 Elsevier | |
| 650 | 7 | |a Parvalbumin |2 Elsevier | |
| 700 | 1 | |a Rao, Qinchun |4 oth | |
| 700 | 1 | |a Jiang, Xingyi |4 oth | |
| 700 | 1 | |a Hsieh, Yun-Hwa Peggy |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Tanaka, Hajime ELSEVIER |t Defining Tumour Shape Irregularity for Preoperative Risk Stratification of Clinically Localised Renal Cell Carcinoma |d 2022 |g Amsterdam [u.a.] |w (DE-627)ELV009139680 |
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10.1016/j.foodcont.2020.107427 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001486.pica (DE-627)ELV051048787 (ELSEVIER)S0956-7135(20)30343-1 DE-627 ger DE-627 rakwb eng 610 VZ Keshavarz, Behnam verfasserin aut Immunochemical analysis of pepsin-digested fish tropomyosin 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. Tropomyosin Elsevier Pepsin digestion Elsevier Epitope mapping Elsevier Fish allergen Elsevier Parvalbumin Elsevier Rao, Qinchun oth Jiang, Xingyi oth Hsieh, Yun-Hwa Peggy oth Enthalten in Elsevier Science Tanaka, Hajime ELSEVIER Defining Tumour Shape Irregularity for Preoperative Risk Stratification of Clinically Localised Renal Cell Carcinoma 2022 Amsterdam [u.a.] (DE-627)ELV009139680 volume:118 year:2020 pages:0 https://doi.org/10.1016/j.foodcont.2020.107427 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 118 2020 0 |
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10.1016/j.foodcont.2020.107427 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001486.pica (DE-627)ELV051048787 (ELSEVIER)S0956-7135(20)30343-1 DE-627 ger DE-627 rakwb eng 610 VZ Keshavarz, Behnam verfasserin aut Immunochemical analysis of pepsin-digested fish tropomyosin 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. Tropomyosin Elsevier Pepsin digestion Elsevier Epitope mapping Elsevier Fish allergen Elsevier Parvalbumin Elsevier Rao, Qinchun oth Jiang, Xingyi oth Hsieh, Yun-Hwa Peggy oth Enthalten in Elsevier Science Tanaka, Hajime ELSEVIER Defining Tumour Shape Irregularity for Preoperative Risk Stratification of Clinically Localised Renal Cell Carcinoma 2022 Amsterdam [u.a.] (DE-627)ELV009139680 volume:118 year:2020 pages:0 https://doi.org/10.1016/j.foodcont.2020.107427 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 118 2020 0 |
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10.1016/j.foodcont.2020.107427 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001486.pica (DE-627)ELV051048787 (ELSEVIER)S0956-7135(20)30343-1 DE-627 ger DE-627 rakwb eng 610 VZ Keshavarz, Behnam verfasserin aut Immunochemical analysis of pepsin-digested fish tropomyosin 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. Tropomyosin Elsevier Pepsin digestion Elsevier Epitope mapping Elsevier Fish allergen Elsevier Parvalbumin Elsevier Rao, Qinchun oth Jiang, Xingyi oth Hsieh, Yun-Hwa Peggy oth Enthalten in Elsevier Science Tanaka, Hajime ELSEVIER Defining Tumour Shape Irregularity for Preoperative Risk Stratification of Clinically Localised Renal Cell Carcinoma 2022 Amsterdam [u.a.] (DE-627)ELV009139680 volume:118 year:2020 pages:0 https://doi.org/10.1016/j.foodcont.2020.107427 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 118 2020 0 |
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10.1016/j.foodcont.2020.107427 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001486.pica (DE-627)ELV051048787 (ELSEVIER)S0956-7135(20)30343-1 DE-627 ger DE-627 rakwb eng 610 VZ Keshavarz, Behnam verfasserin aut Immunochemical analysis of pepsin-digested fish tropomyosin 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. Tropomyosin Elsevier Pepsin digestion Elsevier Epitope mapping Elsevier Fish allergen Elsevier Parvalbumin Elsevier Rao, Qinchun oth Jiang, Xingyi oth Hsieh, Yun-Hwa Peggy oth Enthalten in Elsevier Science Tanaka, Hajime ELSEVIER Defining Tumour Shape Irregularity for Preoperative Risk Stratification of Clinically Localised Renal Cell Carcinoma 2022 Amsterdam [u.a.] (DE-627)ELV009139680 volume:118 year:2020 pages:0 https://doi.org/10.1016/j.foodcont.2020.107427 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 118 2020 0 |
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10.1016/j.foodcont.2020.107427 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001486.pica (DE-627)ELV051048787 (ELSEVIER)S0956-7135(20)30343-1 DE-627 ger DE-627 rakwb eng 610 VZ Keshavarz, Behnam verfasserin aut Immunochemical analysis of pepsin-digested fish tropomyosin 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. Tropomyosin Elsevier Pepsin digestion Elsevier Epitope mapping Elsevier Fish allergen Elsevier Parvalbumin Elsevier Rao, Qinchun oth Jiang, Xingyi oth Hsieh, Yun-Hwa Peggy oth Enthalten in Elsevier Science Tanaka, Hajime ELSEVIER Defining Tumour Shape Irregularity for Preoperative Risk Stratification of Clinically Localised Renal Cell Carcinoma 2022 Amsterdam [u.a.] (DE-627)ELV009139680 volume:118 year:2020 pages:0 https://doi.org/10.1016/j.foodcont.2020.107427 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 118 2020 0 |
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Enthalten in Defining Tumour Shape Irregularity for Preoperative Risk Stratification of Clinically Localised Renal Cell Carcinoma Amsterdam [u.a.] volume:118 year:2020 pages:0 |
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In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. 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immunochemical analysis of pepsin-digested fish tropomyosin |
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Immunochemical analysis of pepsin-digested fish tropomyosin |
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A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. |
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A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. |
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A critical step in determining the allergenicity of a food protein is to study the gastrointestinal digestion resistance, which is an essential characteristic of food allergens due to the preservation of their protein structure and immunoglobulin (Ig) E epitopes. In this study, the immunochemical properties of tropomyosin peptide fragments from Atlantic salmon (Salmo salar) and flathead grey mullet (Mugil cephalus) resulted from pepsin digestion were analyzed. To identify the allergens from salmon and mullet, their IgE- and IgG-binding proteins/peptides were studied using fish-allergic human sera and anti-fish protein monoclonal and polyclonal antibodies. From our results, as the major fish allergen, parvalbumin from both species was recognized in all tested human sera. Tropomyosin-bound IgE was identified in 71% of the tested sera. Antigenicity of intact tropomyosin decreased as a function of pepsin digestion time. The amino acid sequence of mullet tropomyosin was analyzed using a tandem mass spectrometer. Two IgE epitopes on Atlantic salmon tropomyosin alpha-1 were mapped. Overall, tropomyosin was identified as one of the major IgE-binding proteins in both fish species; however, further studies are required to determine the clinical significance of fish tropomyosin as an allergen due to its high homology with human tropomyosin. |
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