A New Synthetic Substrate for Trypsin and its Application to the Determination of the Amino-acid Sequence of Proteins


THE problem of the determination of the amino-acid sequence of a protein would be greatly simplified if methods were available for specifically hydrolyzing peptide bonds involving a particular amino-acid. No satisfactory chemical method of doing this has been found, and the only controlled methods of hydrolysis available at present are digestion by proteolytic enzymes, in particular chymotrypsin and trypsin. It seemed possible that useful results might be obtained if a particular amino-acid side-chain could be modified in such a way as to resemble as closely as possible the side-chain involved in the specificity requirements of some enzyme. If the resemblance could be made sufficiently close, the enzyme might then hydrolyse the adjacent bond.

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  1. 1

    Lindley, H., J. Amer. Chem. Soc., 77, 4927 (1955).

  2. 2

    Waley, S. G., and Watson, J., Biochem. J., 55, 328 (1953).

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