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


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.

Access options

Rent or Buy article

Get time limited or full article access on ReadCube.


All prices are NET prices.


  1. 1

    Hill, R. L., Adv. Prot. Chem., 20, 37 (1965).

  2. 2

    Alvord, E. C., in The Central Nervous System (edit. by Bailey, O. T. and Smith, D. E.), 52 (Williams and Wilkins, Baltimore, 1968).

  3. 3

    Kies, M. W., Ann. NY Acad. Sci., 122, 161 (1965).

  4. 4

    Offord, R. E., Nature, 211, 591 (1966).

  5. 5

    Gray, W. R., in Methods in Enzymology (edit. by Colowick, S. P. Kaplan, N. O. and Hirs, C. H. W.), 11, 469 (1967).

  6. 6

    Eylar, E. H., and Hashim, G. A., Proc. US Nat. Acad. Sci., 61, 644 (1968).

  7. 7

    Carnegie, P. R., Biochem. J., 111, 240 (1969).

  8. 8

    Milstein, C., Clegg, J. B., and Jarvis, J. M., Biochem. J., 110, 631 (1968).

  9. 9

    Milstein, C., FEBS Lett., 2, 301 (1969).

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Cite this article

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

Download citation

Further reading


By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.