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. 1986 Aug 1;237(3):899–906. doi: 10.1042/bj2370899

A systematic series of synthetic chromophoric substrates for aspartic proteinases.

B M Dunn, M Jimenez, B F Parten, M J Valler, C E Rolph, J Kay
PMCID: PMC1147073  PMID: 3541904

Abstract

The hydrolysis of the chromogenic peptide Pro-Thr-Glu-Phe-Phe(4-NO2)-Arg-Leu at the Phe-Phe(4-NO2) bond by nine aspartic proteinases of animal origin and seven enzymes from micro-organisms is described [Phe(4-NO2) is p-nitro-L-phenylalanine]. A further series of six peptides was synthesized in which the residue in the P3 position was systematically varied from hydrophobic to hydrophilic. The Phe-Phe(4-NO2) bond was established as the only peptide bond cleaved, and kinetic constants were obtained for the hydrolysis of these peptide substrates by a representative selection of aspartic proteinases of animal and microbial origin. The value of these water-soluble substrates for structure-function investigations is discussed.

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Selected References

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