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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Allergy to castor bean. II. Identification of the major allergens in castor bean seeds.

Castor bean proteins were separated and identified by isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis and blotted onto nitrocellulose paper. The capacity of the castor bean proteins to bind human IgE was probed with sera from castor bean-sensitive patients and radiolabeled anti-IgE. It proved difficult to identify allergens with isoelectric focusing. However, three allergens were identified when proteins were first separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis: the 2S storage albumin, the 11S crystalloid proteins, and a third protein doublet with molecular weights of 47 and 51 kd. Specific IgE antibody to the 2S storage albumin, measured by RAST, was detected in most (96%) castor bean-sensitive patients, confirming it as the major allergen. We would like to suggest that the 2S albumin be named Ric c I, that the crystalloid proteins be named Ric c II, and that the 47/51 kd doublet be named allergen 3.[1]

References

  1. Allergy to castor bean. II. Identification of the major allergens in castor bean seeds. Thorpe, S.C., Kemeny, D.M., Panzani, R.C., McGurl, B., Lord, M. J. Allergy Clin. Immunol. (1988) [Pubmed]
 
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