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
Oosterbaan, and van Adrichem, Biochim. Biophys. Acta, 27, 423 (1958).
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Porter, Rydon, and Schofield, Nature, 182, 927 (1958). Rydon, ibid., 182, 928 (1958).
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). https://doi.org/10.1038/187596a0
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DOI: https://doi.org/10.1038/187596a0
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