Original title: Molární poměr cytochromu b5 k jeho reduktasam ovlivňuje aktivitu cytochromu P450 1A1 vůči Sudanu I
Translated title: Molar ratio between cytochrome b5 and its reductases affects activity of cytochrome P450 1A1 towards Sudan I
Authors: Netolický, Jakub ; Martínek, Václav (advisor) ; Dračínská, Helena (referee)
Document type: Bachelor's theses
Year: 2017
Language: cze
Abstract: [cze] [eng]
Cytochromy P450 jsou evolučně velmi starou skupinou enzymů, která zahrnuje celou řadu isoforem a její zástupce lze najít u živočichů, rostlin, hub, bakterií i některých virů. Patří mezi enzymy katalyzující první fázi biotransformace léčiv, polutantů a jiných xenobiotik. Právě z tohoto důvodu patří mezi jedny z nejvíce zkoumaných enzymů a je snahou zmapovat jeho účinky na xenobiotika a léky. Cytochrom P450 potřebuje pro svou funkci donory elektronů, mezi hlavní patří NADPH:cytochrom P450 oxidoreduktasa a cytochrom b5. Alternativní reduktasou která v tomto procesu také participuje je NADH:cytochrom b5 oxidoreduktasa, který je schopná redukovat cytochrom b5. Všechny tyto tři enzymy nacházíme v membránách endoplasmatického retikula, kde spolu přirozeně interagují. Tato práce se zaměřuje na aktivitu lidského rekombinantního cytochromu P450 1A1 vůči karcinogennímu azobarvivu Sudan I, konkrétně mapuje tvorbu hlavních metabolitů v závislosti na vzájemném poměru cytochromu b5 k NADPH:cytochrom P450 oxidoreduktase a také k NADH:cytochrom b5 oxidoreduktase. Klíčová slova: cytochrom P450 1A1, NADPH:cytochrom P450 oxidoreduktasa, cytochrom b5, NADH:cytochrom b5 oxidoreduktasa, Sudan I, HPLC Cytochromes P450 are an evolutionary very old group of enzymes. It spread into many isoforms that can be found in animals, plants, fungi, bacteria, and some viruses. They play a major role in the first phase of the biotransformation of drugs, environmental pollutants and other xenobiotics. Also for this reason, they belong among the most researched enzymes. Cytochrome P450 for its function requires an electron donor, such as NADPH:cytochrome P450 oxidoreductase and cytochrome b5. The alternative reductase involved in this process is NADH:cytochrome b5 oxidoreductase, which is able to reduce cytochrome b5. In a eukaryotic cell, all these membrane proteins are found in the endoplasmic reticulum membrane, where they can naturally interact. This work evaluates the activity of human recombinant cytochrome P450 1A1 against the carcinogenic azo dye Sudan I, specifically it focuses on mapping the formation of major metabolites in relation to the ratio of cytochrome b5 to NADPH:cytochrome P450 oxidoreductase as well as to NADH:cytochrome b5 oxidoreductase. Keywords: cytochrome P450 1A1, NADPH:cytochrome P450 oxidoreductase, cytochrome b5, NADH:cytochrome b5 oxidoreductase, Sudan I, HPLC [In Czech]
Keywords: cytochrome b5; cytochrome P450 1A1; HPLC; NADH:cytochrome b5 oxidoreductase; NADPH:cytochrome P450 oxidoreductase; Sudan I; cytochrom P450 1A1; cytochromu b5; HPLC; NADH:cytochrom b5 oxidoreduktasa; NADPH:cytochrom P450 oxidoreduktasa; Sudan I

Institution: Charles University Faculties (theses) (web)
Document availability information: Available in the Charles University Digital Repository.
Original record: http://hdl.handle.net/20.500.11956/87636

Permalink: http://www.nusl.cz/ntk/nusl-364233


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Universities and colleges > Public universities > Charles University > Charles University Faculties (theses)
Academic theses (ETDs) > Bachelor's theses