Acetylation of Trypsin in Organic Solvents

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Abstract

PREVIOUS work in this laboratory has shown that treatment of trypsin with various anhydrides results in the formation of the corresponding acyltrypsin derivatives, each possessing some interesting properties of its own, while all retained their original proteolytic activity1. From the derivatives so far prepared, acetyltrypsin is the best-characterized chemically modified enzyme2, while succinyltrypsin is the most stable of the derivatives so far obtained3. The use of water as a solvent in investigating enzyme modification sets some definite limitations as to type of reagent usable and as to reactions possible. It was with these experiences in mind that the study of acetylation of trypsin was pursued in two organic solvents, formamide and dimethylsulphoxide, Hees and Singer4 having indicated the compatibility of these systems.

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References

  1. 1

    Sri Ram, J., Terminiello, L., Bier, M., and Nord, F. F., Arch. Biochem. Biophys., 52, 464 (1954); 57, 252 (1955). Bier, M., Sri Ram, J., and Nord, F. F., Nature, 176, 789 (1955).

  2. 2

    Nord, F. F., Bier, M., and Terminiello, L., Arch. Biochem. Biophys., 65, 120 (1956). Uraki, Z., Terminiello, L., Bier, M., and Nord, F. F., Arch. Biochem. Biophys., 69, 644 (1957).

  3. 3

    Terminiello, L., Bier, M., and Nord, F. F., Arch. Biochem. Biophys., 73, 171 (1958).

  4. 4

    Rees, E. D., and Singer, S. J., Arch. Biochem. Biophys., 63, 144 (1956).

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VRATSANOS, S., BIER, M. & NORD, F. Acetylation of Trypsin in Organic Solvents. Nature 181, 414–415 (1958) doi:10.1038/181414a0

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