Abstract
A water-soluble, heat-stable protein component of castor seed meal was subjected to paper-strip electrophoresis in buffers of different chemical composition, pH values, and ionic strengths. It was shown that phosphate buffer at pH 7.4 to 8.0 and an ionic strength of approximately 0.05 gave a sharp resolution of castor seed proteins into bands which would bind bromophenol blue. Spies' Allergen CB-1A was shown to be resolved into six or more components at pH 8.0. Each major component band was found to be antigenic by passive cutaneous anaphylaxis in guinea pigs that were sensitized with rabbit antiserum to the crude castor seed protein preparation. Five bands were shown to be allergenic to humans.
The results appear to support earlier observations (1,2,10) that castor bean seed allergenicity to humans may be caused by more than one antigen in Spies' Allergen CB-1A and possibly by other antigens present in the seed but either absent from, or greatly reduced in concentration in, allergen CB-1A.
The water-soluble component of Altschul's active castor seed lipase was resolved into eight component bands, two of which did not appear in the electrophotograms of the heat-processed preparation CB-1A S.R.I.
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A laboratory of the Western Utilization Research and Development Division, Agricultural Research Service, U.S. Department of Agriculture.
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Layton, L.L., Dante, B.T., Moss, L.K. et al. Electrophoretic fractionation of soluble antigenic proteins from the seed ofRicinus communis (castor bean). J Am Oil Chem Soc 38, 405–410 (1961). https://doi.org/10.1007/BF02637975
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DOI: https://doi.org/10.1007/BF02637975