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). 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.
Lehrer
S B
SB
Department of Medicine, Tulane University School of Medicine, New Orleans, La 70112.
Ibanez
M D
MD
McCants
M L
ML
Daul
C B
CB
Morgan
J E
JE
D000485:Allergens / Q000032:analysis; D000818:Animals; D000918:Antibody Specificity; D033364:Decapoda / Q000276:immunology*; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology; D011852:Radioallergosorbent Test; D012995:Solubility; D014867:Water
D000485:Allergens; D014867:Water; D007073:Immunoglobulin E