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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POULIK, M., SHUSTER, J. Heterogeneity of H Chains of Myeloma Proteins : Susceptibility to Papain and Trypsin. Nature 204, 577–579 (1964). https://doi.org/10.1038/204577a0
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DOI: https://doi.org/10.1038/204577a0
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