Klonování a exprese lidské AKR1A1

Charles University in Prague Faculty of Pharmacy in Hradec Králové Department of Biochemical Sciences Candidate: Petra Kořínková Supervisor: Prof. Ing. Vladimír Wsól, Ph.D. Title of diploma thesis: Cloning and expression of human AKR1A1 The aldo-keto reductase 1A1 (AKR1A1) is monomeric cytosolic enz...

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Bibliographic Details
Main Author: Kořínková, Petra
Other Authors: Wsól, Vladimír
Format: Dissertation
Language:Czech
Published: 2013
Online Access:http://www.nusl.cz/ntk/nusl-324209
Description
Summary:Charles University in Prague Faculty of Pharmacy in Hradec Králové Department of Biochemical Sciences Candidate: Petra Kořínková Supervisor: Prof. Ing. Vladimír Wsól, Ph.D. Title of diploma thesis: Cloning and expression of human AKR1A1 The aldo-keto reductase 1A1 (AKR1A1) is monomeric cytosolic enzyme from aldo- keto reductase superfamily (AKR) with carbonyl reducing activity. The members of AKR superfamily have an important role in reductive reactions in metabolism of some endogenous substrates and in the first phase of biotransformation of xenobiotics. Fifteen members of this large family have been found in the human body. These proteins are expressed in different tissues within all our organism. The highest concentrations of proteins have been detected in the hepatocytes and in the renal cells. The function of AKR1A1 is to catalyse reductive reactions of aromatic and aliphatic aldehydes to the respective alcohols. Among its important substrates belong mevalonate (endogenous substance) and some drugs like anthracykline antibiotics - doxorubicin and daunorubicin. AKR1A1 also participates in biotransformations of sorbitol and in the development of diabetes complications. Preparation of recombinant protein was performed in E. coli with using of pET28b(+) as an expression vector. Isolated cDNA was...