Abstract
Human α 2-macroglobulin has been digested with papain (EC 3.4.4.10) at pH values of 5.7 and below to give an immunologically detectable, low-molecular-weight component ( s 20, w approx. 3 S). The digestion process also results in the liberation of a considerable amount of peptide material. Digestion appears to proceed by a series of components of intermediate starchgel electrophoretic mobility, the final component moving in the post-albumin position. Gel diffusion studies reveal that the product is deficient in primate specific antigenic groupings, but carries the antigenic determinants responsible for its cross reactivity with the α 2-macroglobulin homologues of other mammalian species.
Published Version
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