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.
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