Structures of Some Acetyl-serine Peptides from Acetyl-chymotrypsin

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Abstract

IN 1958, two of us1 obtained, by enzymic degradation of acetyl-chymotrypsin labelled with carbon-142, five peptides containing labelled acetyl-groups. Subsequent sequence studies3 have shown that the largest of these peptides has the amino-acid sequence, Gly.Asp.Ser.Gly.Gly.Pro.Leu, identical with that already found4, by degradation of the di-isopropylphosphoryl-enzyme, to surround the reactive serine ; it may reasonably be concluded that the other four peptides contain the sequences Ser.Gly.Gly.Pro.Leu, Asp.Ser.Gly.Gly, Gly.Asp.Ser.Gly and Ser.Gly.Gly, respectively.

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References

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    Oosterbaan, and van Adrichem, Biochim. Biophys. Acta, 27, 423 (1958).

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    Jansz, Berends, and Oosterbaan, Rec. Trav. Chim., 78, 876 (1959). Cohen, Oosterbaan, Jansz, and Berends, J. Cell. Comp. Physiol., 54, Supp. 1, 231 (1959).

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    Oosterbaan, Jansz, and Cohen, Biochim. Biophys. Acta, 20, 402 (1956). Oosterbaan, Kunst, van Rotterdam, and Cohen, ibid., 27, 549, 556 (1958).

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    Benoiton, and Rydon, J. Chem. Soc. (in the press).

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    Porter, Rydon, and Schofield, Nature, 182, 927 (1958). Rydon, ibid., 182, 928 (1958).

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    For references, see the review by Davies and Green, “Adv. Enzymol.”, 20, 283 (1958).

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BENOITON, L., RYDON, H., OOSTERBAAN, R. et al. Structures of Some Acetyl-serine Peptides from Acetyl-chymotrypsin. Nature 187, 596–597 (1960) doi:10.1038/187596a0

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