Skip to main content
Log in

Electrophoretic fractionation of soluble antigenic proteins from the seed ofRicinus communis (castor bean)

  • Technical
  • Published:
Journal of the American Oil Chemists Society

    We’re sorry, something doesn't seem to be working properly.

    Please try refreshing the page. If that doesn't work, please contact support so we can address the problem.

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Layton, L.L., Moss, L.K., and DeEds, F., Federation Proc.,19, No. 1, A-195 (1960).

    Google Scholar 

  2. Layton, L.L., Mose, L.K., and DeEds, F., J. Am. Oil Chemists' Soc.,38, 76–80 (1961).

    Article  CAS  Google Scholar 

  3. Coulson, E.J., J. Allergy,24, No. 5, 458 (1953).

    Article  PubMed  CAS  Google Scholar 

  4. Spies, J.R., and Coulson, E.J., J. Am. Chem. Soc.,65, 1720 (1943).

    Article  CAS  Google Scholar 

  5. Spies, J.R., Coulson, E.J., Chambers, D.C., Bernton, H.S., Stevens, H., and Shimp, J.H., J. Am. Chem. Soc.,73, 3995 (1951).

    Article  CAS  Google Scholar 

  6. Spies, J.R., Coulson, E.J., Chambers, D.C., Bernton, H.S., and Stevens, H., J. Am. Chem. Soc.,66, 748 (1944).

    Article  CAS  Google Scholar 

  7. Coulson, E.J., Spies, J.R., Stevens, H., and Shimp, J.H., J. Allergy,21, No. 1, 34 (1950).

    Article  PubMed  CAS  Google Scholar 

  8. Layton, L.L., and DeEds, F., to be published.

  9. Layton, L.L. Lee, S., Dante, B.T., and DeEds, F., to be published.

  10. Layton, L.L., Lee, S., and DeEds, F., Federation Proc.,20, No. 1, Part 1, 17 (1961).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

A laboratory of the Western Utilization Research and Development Division, Agricultural Research Service, U.S. Department of Agriculture.

About this article

Cite this article

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

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02637975

Keywords

Navigation