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- W2076342875 abstract "Dipeptidyl peptidase III (EC 3.4.14.4) was purified from porcine skeletal muscle by ammonium sulfate fractionation and by chromatography and rechromatography on a Biosept-DEAE HPLC column. The enzyme was purified 2329-fold with a 19% recovery. The relative molecular mass was estimated to be 82 000 Da by SDS−PAGE and the maximum activity was reached at pH 8.0 and 40 °C. The enzyme had a wider range of hydrolysis on peptide substrates than over dipeptidyl-AMC derivatives, but without any endopeptidase activity. On the basis of the kinetic parameters and the substrates studied, the tetrapeptide Gly-Gly-Phe-Leu (des-Tyr1 Leu-enkephalin) showed the best affinity for DPP III. The serine peptidase inhibitor 3,4-DCI, along with the cysteine protease inhibitors p-CMB and DTNB were potent inhibitors of DPP III. Chelating and reducing agents also affected considerably the enzyme activity. Co2+ was proved to markedly increase the enzyme activity. Zn2+, Fe2+, Cu2+, Cd2+, and Hg2+ inhibited the activity, while Ca2+ and Mg2+ had no effect. The dipeptide Tyr-Tyr exerted an important inhibitory effect on DPP III activity. Keywords: Dipeptidyl peptidase III; muscle; purification; peptide hydrolysis; capillary electrophoresis; HPLC" @default.
- W2076342875 created "2016-06-24" @default.
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- W2076342875 date "1998-09-30" @default.
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- W2076342875 title "Biochemical Properties of Dipeptidyl Peptidase III Purified from Porcine Skeletal Muscle" @default.
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- W2076342875 doi "https://doi.org/10.1021/jf980356i" @default.
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