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Heterogeneity of H Chains of Myeloma Proteins : Susceptibility to Papain and Trypsin

Nature volume 204, pages 577579 (07 November 1964) | Download Citation

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Abstract

PROTEOLYTIC digestion of proteins has been one of the methods used in determining protein structure1–3. Closely allied proteins such as γ-globulins revealed after enzyme cleavage significant differences in products. It was shown that the main fragments (S and F) of normal human 7S γ-globulins obtained by papain digestion are heterogeneous4–6. These investigations were now extended to abnormal γ-globulins (7S and β2A myeloma γ-globulins) in order to compare the structural make-up of the sub-components of their S and F fragments. During the course of the investigation an F fragment, extremely labile to proteolytic digestions, was found in one of the 7S myeloma γ-globulins studied.

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Affiliations

  1. Child Research Center of Michigan, Detroit 2, and Department of Pediatrics, Wayne State University School of Medicine, Detroit 7, Michigan.

    • M. D. POULIK
    •  & J. SHUSTER

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https://doi.org/10.1038/204577a0

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