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• W2996013659 endingPage "113557" @default.
• W2996013659 startingPage "113557" @default.
• W2996013659 abstract "Dipeptidyl peptidase IV (DPP-IV) is an aminopeptidase that cleaves the N-terminal dipeptide from peptides bearing proline or alanine residues. Currently, DPP-IV activity is quantified by spectrophotometric or fluorometric methods, which employ Gly-Pro-pNA and Gly-Pro-AMC respectively, as substrate. However, these methods require high enzyme and substrate concentrations. In this study, we adapted the DPP-IV fluorospectrometric assay using NanoDrop 3300, which requires only nanogram levels of the enzyme (30 ng crude DPP-IV) and considerably low substrate concentrations (100 μM). Fluorescence measurement required a reaction mixture of only 2 μL, thus eliminating the need for microtiter plates or cuvettes.We employed this assay to demonstrate DPP-IV activity in porcine serum for the first time. The enzymatic activity peaked at pH 8.0 in porcine (84 nM/min), human (87 nM/min) and bovine (89.1 nM/min) sera, with the optimum temperature of 37 °C. The enzyme showed maximum activity upon incubation for 40 min at 37 °C. In contrast, activity in the porcine serum was the highest after incubation for 30 min at the same optimized parameters. The IC50 values of diprotin A against DPP-IV from human, porcine, and bovine sera were 7.83, 8.62, 9.17 μM, respectively. The present assay procedure is a convenient, sensitive, accurate and high-throughput method suitable for primary screening of DPP-IV inhibitors." @default.
• W2996013659 created "2019-12-26" @default.
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• W2996013659 date "2020-03-01" @default.
• W2996013659 modified "2023-10-14" @default.
• W2996013659 title "Rapid detection of DPP-IV activity in porcine serum: A fluorospectrometric assay" @default.
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• W2996013659 doi "https://doi.org/10.1016/j.ab.2019.113557" @default.
• W2996013659 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31866290" @default.
• W2996013659 hasPublicationYear "2020" @default.
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