Record Display for the EPA National Library Catalog


OLS Field Name OLS Field Data
Main Title Isolation of hayfever antigens from short ragweed pollen /
Author Flora, Robert M.
CORP Author Worthington Biochemical Corp., Freehold, N.J.;National Environmental Research Center, Research Triangle Park, N.C. Chemistry and Physics Lab.
Publisher Office of Research and Development, U.S. Environmental Protection Agency ; Available from National Technical Information Service,
Year Published 1974
Report Number 68-02-0566; EPA-650/2-74-044; EPA-68-02-0566
Stock Number PB-237691
OCLC Number 37575645
Subjects Antigens. ; Allergens. ; Ragweeds--Pollen.
Additional Subjects Hay fever ; Pollen ; Antigens ; Aerobiology ; Isolation ; Chemical analysis ; Biochemistry ; Electrophoresis ; Chromatography ; Precipitation(Chemistry) ; Ragweed ; Ambrosia ; Allergens ; Immunodiffusion ; Immunoelectrophoresis ; Ouchterlony technique
Internet Access
Description Access URL
Library Call Number Additional Info Location Last
ELBD RPS EPA 650-2-74-044 2 repository copies AWBERC Library/Cincinnati,OH 04/20/2020
ELBD RPS EPA 650-2-74-044 repository copy AWBERC Library/Cincinnati,OH 05/10/2020
NTIS  PB-237 691 Most EPA libraries have a fiche copy filed under the call number shown. Check with individual libraries about paper copy. 01/01/1988
Collation volumes (various pagings) : illustrations ; 28 cm.
Antigen E was prepared in pure form while both of the minor antigens, K and Ra3, were not processed to purity. Twenty kilograms of pollen were defatted and extracted with water. The antigens were then isolated by salt precipitation and column chromatography. The process was monitored with electrophoresis and immune precipitin tests. The final bulk of antigen E obtained was tested for purity and lyophilized before shipment. Total yield was 5.4g of pure antigen E and approximately 374g of the side fractions containing K and Ra3. Micro-Ouchterlony tests of antigen E gave a single precipitin line with anti-antigen E serum. Immunoelectrophoresis resulted in a triphasic precipitin band corresponding to the three bands obtained in polyacrylamide gel electrophoresis. UV absorption scans of the antigen E showed a typical protein peak at 280 nm wavelength, and micro-Kjeldahl analysis gave a nitrogen content of 15.4%. All test results were compatible with published reports and indicated that the antigen E prepared meets a high degree of purity.
Performed by Worthington Biochemical Corporation under EPA contract no. 68-02-0566, program element no. 1AA010. "April 1974." "EPA-650/2-74-044." Project officer: Eva Wittgenstein. Includes bibliographical references.