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Abstract
Antigenic relationships of previously described electrophoretic fractionation products of the allergenic protein-carbohydrate fraction CS-1A from cottonseed were studied by the Dale method. Fraction CS-51R (picric acid-precipitable cathodic fraction) was found to be antigenically indistinguishable from CS-56R (picric acid-precipitable anodic fraction). Fraction CS-56S, separated from the mother liquor in the picric acid fractionation of the anodic fraction, was found to contain antigen unrelated to CS-51R or CS-56R. A refractionated carbohydrate-free cathodic fraction, CS-60C, was antigenically indistinguishable from CS-51R. Hence carbohydrate plays no apparent role in determining antigenic specificity.
The antigenic specificity of fractions CS-51R and CS-56R was not altered by the procedure of isolation. Thus they appear to be preformed native proteins.
Footnotes
1 Contribution from Allergen Investigations, Bureau of Agricultural and Industrial Chemistry, Agricultural Research Administration, U. S. Department of Agriculture.
2 For paper I of this series see Coulson, Spies and Stevens, This Journal 1941, 41: 375.
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