1964
DOI: 10.1021/bi00891a026
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Isolation and Characterization of Allergens from Ragweed Pollen. II*

Abstract: designated as IV and was isolated from pollen extracts by ammonium sulfate precipitation followed with DEAE-cellulose1 and Sephadex chromatography. Immunodiffusion studies of fraction IV with rabbit antiragweed sera showed that it contained a principal component which was called antigen E. However

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Cited by 248 publications
(89 citation statements)
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“…500-1000 times higher than required with the > 10-kD protein allergens (data not shown). The decrease of IgE binding by the depigmented ragweed pollen proteins is probably due to the lability of IgE-specific peptide epitopes at low pH values, as already reported by King et al for ragweed antigen E [17].…”
Section: Discussionsupporting
confidence: 73%
“…500-1000 times higher than required with the > 10-kD protein allergens (data not shown). The decrease of IgE binding by the depigmented ragweed pollen proteins is probably due to the lability of IgE-specific peptide epitopes at low pH values, as already reported by King et al for ragweed antigen E [17].…”
Section: Discussionsupporting
confidence: 73%
“…In all of the analyses of IgE and IgG antibodies to AgE the same lot of partially purified AgE was utilized. In the remainder of this paper the term AgE will refer to this partially purified preparation, and AgE IV-C 2 will be used to designate the more highly purified protein of King, Norman, and Connell (14). After thorough washing to remove noncovalently bound AgE, the cellulose-AgE polymer was suspended at a concentration of 1 mg/ml in 0. again with pH 4.0 0.1 M sodium acetic acid, and a third time with borate-saline.…”
Section: Methodsmentioning
confidence: 99%
“…The best known allergens, AgE and AgK of ragweed pollen, contain no carbohydrate (11,12). However, the involvement of the carbohydrate in antigenicity has been repeatedly demonstrated (13)(14)(15)(16).…”
Section: Structure Bmentioning
confidence: 99%