Characterization of water-soluble shrimp allergens released during boiling
Water-soluble shrimp allergens released during boiling (shrimp water) were characterized and compared to allergen extracts from boiled shrimp (shrimp meat). Both shrimp extracts contained acidic proteins (isoelectrofocusing) and demonstrated similar allergenic activity (RAST and RAST inhibition). Sh...
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Published in | Journal of allergy and clinical immunology Vol. 85; no. 6; pp. 1005 - 1013 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Mosby, Inc
01.06.1990
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Subjects | |
Online Access | Get full text |
ISSN | 0091-6749 |
DOI | 10.1016/0091-6749(90)90044-5 |
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Abstract | Water-soluble shrimp allergens released during boiling (shrimp water) were characterized and compared to allergen extracts from boiled shrimp (shrimp meat). Both shrimp extracts contained acidic proteins (isoelectrofocusing) and demonstrated similar allergenic activity (RAST and RAST inhibition). Shrimp-water extract was analyzed further by immunoprinting with sera from 14 shrimp-sensitive, RAST-positive subjects, and six nonsensitive, RAST-negative individuals. Although none of the sera from shrimp-tolerant individuals reacted,
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sera (85.7%) from shrimp-sensitive subjects reacted with shrimp-water proteins with acid isoelectric points. Shrimp-water extract was fractionated by chromatofocusing with pH and NaCl gradients. A number of eluted ultraviolet-absorbing peaks contained allergens as determined by RAST inhibition. Isoelectrofocusing demonstrated many protein bands present in these peaks, some of which bound IgE from a RAST-positive sera pool. These studies indicate that shrimp water is an excellent source of shrimp allergens, that chromatofocusing is a useful method for fractionation of shrimp allergens, and that shrimp allergens are generally protein molecules with acid isoelectric points. |
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AbstractList | Water-soluble shrimp allergens released during boiling (shrimp water) were characterized and compared to allergen extracts from boiled shrimp (shrimp meat). Both shrimp extracts contained acidic proteins (isoelectrofocusing) and demonstrated similar allergenic activity (RAST and RAST inhibition). Shrimp-water extract was analyzed further by immunoprinting with sera from 14 shrimp-sensitive, RAST-positive subjects, and six nonsensitive, RAST-negative individuals. These studies indicate that shrimp water is an excellent source of shrimp allergens, that chromatofocusing is a useful method for fractionation of shrimp allergens, and that shrimp allergens are generally protein molecules with acid isoelectric points. Water-soluble shrimp allergens released during boiling (shrimp water) were characterized and compared to allergen extracts from boiled shrimp (shrimp meat). Both shrimp extracts contained acidic proteins (isoelectrofocusing) and demonstrated similar allergenic activity (RAST and RAST inhibition). Shrimp-water extract was analyzed further by immunoprinting with sera from 14 shrimp-sensitive, RAST-positive subjects, and six nonsensitive, RAST-negative individuals. Although none of the sera from shrimp-tolerant individuals reacted, 12 14 sera (85.7%) from shrimp-sensitive subjects reacted with shrimp-water proteins with acid isoelectric points. Shrimp-water extract was fractionated by chromatofocusing with pH and NaCl gradients. A number of eluted ultraviolet-absorbing peaks contained allergens as determined by RAST inhibition. Isoelectrofocusing demonstrated many protein bands present in these peaks, some of which bound IgE from a RAST-positive sera pool. These studies indicate that shrimp water is an excellent source of shrimp allergens, that chromatofocusing is a useful method for fractionation of shrimp allergens, and that shrimp allergens are generally protein molecules with acid isoelectric points. Water-soluble shrimp allergens released during boiling (shrimp water) were characterized and compared to allergen extracts from boiled shrimp (shrimp meat). Both shrimp extracts contained acidic proteins (isoelectrofocusing) and demonstrated similar allergenic activity (RAST and RAST inhibition). Shrimp-water extract was analyzed further by immunoprinting with sera from 14 shrimp-sensitive, RAST-positive subjects, and six nonsensitive, RAST-negative individuals. Although none of the sera from shrimp-tolerant individuals reacted, 12/14 sera (85.7%) from shrimp-sensitive subjects reacted with shrimp-water proteins with acid isoelectric points. Shrimp-water extract was fractionated by chromatofocusing with pH and NaCl gradients. A number of eluted ultraviolet-absorbing peaks contained allergens as determined by RAST inhibition. Isoelectrofocusing demonstrated many protein bands present in these peaks, some of which bound IgE from a RAST-positive sera pool. These studies indicate that shrimp water is an excellent source of shrimp allergens, that chromatofocusing is a useful method for fractionation of shrimp allergens, and that shrimp allergens are generally protein molecules with acid isoelectric points. Water-soluble shrimp allergens released during boiling (shrimp water) were characterized and compared to allergen extracts from boiled shrimp (shrimp meat). Both shrimp extracts contained acidic proteins (isoelectrofocusing) and demonstrated similar allergenic activity (RAST and RAST inhibition). Shrimp-water extract was analyzed further by immunoprinting with sera from 14 shrimp-sensitive, RAST-positive subjects, and six nonsensitive, RAST-negative individuals. Although none of the sera from shrimp-tolerant individuals reacted, 12/14 sera (85.7%) from shrimp-sensitive subjects reacted with shrimp-water proteins with acid isoelectric points. Shrimp-water extract was fractionated by chromatofocusing with pH and NaCl gradients. A number of eluted ultraviolet-absorbing peaks contained allergens as determined by RAST inhibition. Isoelectrofocusing demonstrated many protein bands present in these peaks, some of which bound IgE from a RAST-positive sera pool. These studies indicate that shrimp water is an excellent source of shrimp allergens, that chromatofocusing is a useful method for fractionation of shrimp allergens, and that shrimp allergens are generally protein molecules with acid isoelectric points.Water-soluble shrimp allergens released during boiling (shrimp water) were characterized and compared to allergen extracts from boiled shrimp (shrimp meat). Both shrimp extracts contained acidic proteins (isoelectrofocusing) and demonstrated similar allergenic activity (RAST and RAST inhibition). Shrimp-water extract was analyzed further by immunoprinting with sera from 14 shrimp-sensitive, RAST-positive subjects, and six nonsensitive, RAST-negative individuals. Although none of the sera from shrimp-tolerant individuals reacted, 12/14 sera (85.7%) from shrimp-sensitive subjects reacted with shrimp-water proteins with acid isoelectric points. Shrimp-water extract was fractionated by chromatofocusing with pH and NaCl gradients. A number of eluted ultraviolet-absorbing peaks contained allergens as determined by RAST inhibition. Isoelectrofocusing demonstrated many protein bands present in these peaks, some of which bound IgE from a RAST-positive sera pool. These studies indicate that shrimp water is an excellent source of shrimp allergens, that chromatofocusing is a useful method for fractionation of shrimp allergens, and that shrimp allergens are generally protein molecules with acid isoelectric points. |
Author | Ibanez, M.D. Lehrer, S.B. Morgan, J.E. McCants, M.L. Daul, C.B. |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/2355151$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1016_S1081_1206_10_60888_5 crossref_primary_10_1046_j_1365_2222_1998_00301_x crossref_primary_10_4049_jimmunol_175_12_8354 crossref_primary_10_1007_BF02914471 crossref_primary_10_1016_0097_3165_93_90015_Z crossref_primary_10_1016_0924_2244_93_90072_I crossref_primary_10_1016_S0335_7457_97_80205_5 crossref_primary_10_1016_S1382_6689_97_10042_4 crossref_primary_10_1111_j_1398_9995_1995_tb02499_x crossref_primary_10_3389_falgy_2021_769728 crossref_primary_10_1111_j_1399_3038_1992_tb00046_x crossref_primary_10_1016_S1081_1206_10_62837_2 crossref_primary_10_1016_S1081_1206_10_62572_0 crossref_primary_10_1080_10408399609527762 crossref_primary_10_1080_10408399609527761 crossref_primary_10_1111_j_1365_2222_1993_tb00359_x crossref_primary_10_1016_S0889_8561_05_70261_7 crossref_primary_10_1016_S0033_8389_22_00230_5 crossref_primary_10_1007_BF02539112 crossref_primary_10_1007_BF02802288 crossref_primary_10_4049_jimmunol_1601334 crossref_primary_10_1016_S0335_7457_01_80013_7 |
Cites_doi | 10.1016/0091-6749(87)90121-7 10.1016/0091-6749(84)90256-2 10.1111/j.1365-2222.1978.tb00446.x 10.1159/000234418 10.4049/jimmunol.138.12.4169 10.1016/0091-6749(86)90173-9 10.1016/0091-6749(81)90041-5 10.1016/0019-2791(72)90112-7 10.1016/0091-6749(89)90474-0 10.1159/000232110 10.1056/NEJM198005153022005 10.1016/0091-6749(85)90724-9 10.1016/0091-6749(82)90079-3 10.1016/S0091-6749(86)80087-2 10.1016/0019-2791(75)90080-4 10.1016/0091-6749(87)90293-4 |
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Snippet | Water-soluble shrimp allergens released during boiling (shrimp water) were characterized and compared to allergen extracts from boiled shrimp (shrimp meat).... |
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SubjectTerms | ALERGENOS ALERGIA ALIMENTARIA ALLERGENE ALLERGENS Allergens - analysis ALLERGIE ALIMENTAIRE analysis Animals Antibody Specificity BOILING CAMARON DE MAR CREVETTE CUISSON A L'EAU Decapoda Decapoda (Crustacea) Decapoda (Crustacea) - immunology EBULLICION EXTRACTION FOOD ALLERGIES Humans HYPERSENSITIVITY Immunoglobulin E Immunoglobulin E - immunology immunologic techniques IMMUNOLOGICAL TECHNIQUES immunology IMMUNOPRINTING Marine PRAWNS Radioallergosorbent Test RADIOIMMUNOASSAY RAST REACCIONES ALERGICAS REACTION ALLERGIQUE seafoods shrimp SHRIMP MEAT SHRIMP WATER Solubility TECHNIQUE IMMUNOLOGIQUE TECHNIQUE RADIOIMMUNOLOGIQUE TECNICAS INMUNOLOGICAS TECNICAS RADIOINMUNOLOGICAS Water |
Title | Characterization of water-soluble shrimp allergens released during boiling |
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