Abstract
IT is well known that the proteolytic enzyme trypsin fails to hydrolyse native proteins, or hydrolyses them to only a very small extent. The denaturation of protein substrate is therefore a customary preliminary operation in all work involving the action of trypsin on proteins. We report here the effect of trypsin on some chemical derivatives of a pure de-ionized1 Bence-Jones protein isolated in large amounts from the urine of a single patient.
Similar content being viewed by others
Article PDF
References
Timasheff, S. N., Dintzis, H. M., Kirkwood, J. G., and Coleman, B. D., J. Amer. Chem. Soc., 79, 782 (1957).
Harrington, W. F., and Schellman, J. A., C.R. Trav. Lab., Carlsberg, Sér. chim., 30, 21 (1956).
Bailey, J. L., and Cole, R. D., J. Biol. Chem., 234, 1733 (1959).
White, jun., F. H., J. Biol. Chem., 235, 383 (1960).
Stauff, J., and Duden, R., Biochem. Z., 331, 10 (1958).
Sela, M., White, jun., F. H., and Anfinsen, C. B., Biochim. Biophys. Acta, 31, 417 (1959).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
FERRINI, U., ZITO, R. Action of Trypsin on Bence-Jones Protein Derivatives. Nature 189, 485 (1961). https://doi.org/10.1038/189485a0
Issue Date:
DOI: https://doi.org/10.1038/189485a0
Comments
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.
