Publication detail

OPTIMIZATION OF CONDITIONS FOR DETERMINING PROLYL OLIGOPEPTIDASE ACTIVITY

Authors: Štěpánková Šárka | Zachrdlová Daniela

Year: 2025

Type of publication: ostatní - článek ve sborníku

Name of source: ChemZi

Publisher name: Slovenská chemická spoločnosť pri SAV

Place: Bratislava

Page from-to: nestránkováno

Titles:

Language	Name	Abstract	Keywords
eng	OPTIMIZATION OF CONDITIONS FOR DETERMINING PROLYL OLIGOPEPTIDASE ACTIVITY	Prolyl oligopeptidase (POP) is a serine protease found in almost all tissues of the human body, with the highest activity in skeletal muscle and brain. Its main function is to cleave small peptides at the carboxyl side of the proline residue. Some studies suggest that POP may be associated with neurodegeneration, memory and cognitive impairment. Patients with Alzheimer's disease have been found to have significantly higher levels of POP activity than healthy individuals. Inhibition of POP may improve memory by blocking the metabolism of endogenous neuropeptides. The aim of the work was to determine suitable conditions for measuring POP activity, specifically the effect of temperature, substrate concentration and enzyme amount on the reaction rate was investigated. The determination of POP activity is based on the hydrolysis of the substrate Z-Gly-Pro-4-nitroanilide. The formation of p-nitroanilide, directly proportional to POP activity, was measured spectrophotometrically at 405 nm and the rate of the enzymatic reaction under given conditions was subsequently determined. From the dependence of the reaction rate on the substrate concentration and the amount of enzyme at selected temperatures, suitable conditions for measuring the activity and possibly inhibition of POP were determined. Kinetic parameters, KM and Vm were also determined.	prolyl oligopeptidase; kinetics; activity

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