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OPTIMIZATION OF CONDITIONS FOR DETERMINING PROLYL OLIGOPEPTIDASE ACTIVITY

Autoři: Štěpánková Šárka | Zachrdlová Daniela

Rok: 2025

Druh publikace: ostatní - článek ve sborníku

Název zdroje: ChemZi

Název nakladatele: Slovenská chemická spoločnosť pri SAV

Místo vydání: Bratislava

Strana od-do: nestránkováno

Tituly:

Jazyk	Název	Abstrakt	Klíčová slova
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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