| 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 |
|
| Holdings |
| Library |
Call Number |
Additional Info |
Location |
Last
Modified |
Checkout
Status |
| ELBD RPS |
EPA 650-2-74-044 |
2 repository copies |
AWBERC Library/Cincinnati,OH |
04/20/2020 |
| NTIS |
PB-237 691 |
Some EPA libraries have a fiche copy filed under the call number shown. |
|
07/26/2022 |
|
| Collation |
volumes (various pagings) : illustrations ; 28 cm. |
| Abstract |
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. |
| Notes |
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. |
