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.
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).
About this article
Archives of Biochemistry and Biophysics (1964)
The Lancet (1962)