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Digestion of an Arg–Pro Bond by Trypsin in the Encephalitogenic Basic Protein of Human Myelin

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Abstract

MOST bonds in proteins involving the sequence Arg-X or Lys-X are readily digested by trypsin, but where X is proline no digestion is assumed to occur. This assumption is based on numerous reports on the failure of trypsin to split such bonds in proteins and peptides1. In this article the hydrolysis of an Arg-Pro bond by trypsin in the basic protein of human myelin is described. This protein in doses of 1 µg (60 pmoles) in Freund's complete adjuvant is able to induce the disease “experimental autoimmune encephalomyelitis” in guinea-pigs2.

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Authors and Affiliations

  1. Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, 3052, Australia

    P. R. CARNEGIE

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  1. P. R. CARNEGIE
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CARNEGIE, P. Digestion of an Arg–Pro Bond by Trypsin in the Encephalitogenic Basic Protein of Human Myelin. Nature 223, 958–959 (1969). https://doi.org/10.1038/223958a0

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  • DOI: https://doi.org/10.1038/223958a0

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