Abstract
PORTER1has shown that antibodies can be digested with papain to yield univalent fragments, molecular weight about 50,000, and an inactive fragment, molecular weight 80,000. The univalent fragments obtained are separable by chromatography on carboxymethylcellulose (CMC) into two fractions called Fraction I and Fraction II. Since then, Stelos et al.2have shown that the fragments in each fraction come from different antibody molecules (see also Palmer et al.3). We have also been able to show that fragments of Fraction I and fragments of Fraction II can be further fractionated and that the fragments in the various fractions appear to be different on a chemical basis also2. We showed that in the case of specifically purified antibody against the azobenzoate ion and azobenzenearsonate ion the rates of iodination of the fragments appearing in Fraction I are different from those appearing in Fraction II. This was demonstrated by iodinating the mixture of fragments and then chromatographing it. It was found that the iodine–protein ratio was different for the two fractions. On the other hand, the rates of iodination of the fragments of Fraction I and of Fraction II from normal γ-globulin were usually quite similar. The results of this experiment indicate that not only were there chemical differences between the fragments in Fraction I and in Fraction II from a specifically purified antibody, but also that these molecules differed from normal γ-globulin.
Published Version
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