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Sunday, July 26, 2020 | History

3 edition of Exploring the Functional Plasticity of Human Glutathione Transferases found in the catalog.

Exploring the Functional Plasticity of Human Glutathione Transferases

Ann-Sofie Johansson

Exploring the Functional Plasticity of Human Glutathione Transferases

Allelic Variants, Novel Isoenzyme & Enzyme Redesign (Comprehensive Summaries of ... the Faculty of Science and Technology, 695)

by Ann-Sofie Johansson

  • 88 Want to read
  • 22 Currently reading

Published by Uppsala Universitet .
Written in English

    Subjects:
  • Life Sciences - Biochemistry,
  • Science,
  • Science/Mathematics

  • The Physical Object
    FormatPaperback
    Number of Pages56
    ID Numbers
    Open LibraryOL12854482M
    ISBN 109155452701
    ISBN 109789155452704
    OCLC/WorldCa185982741

      Reactive oxygen or nitrogen species are generated in the plant cell during the extreme stress condition, which produces toxic compounds after reacting with the organic molecules. The glutathione-S-transferase (GST) enzymes play a significant role to detoxify these toxins and help in excretion or sequestration of them. In the present study, we have cloned bp long promoter . Glutathione S -transferases (GSTs) have been well documented to be involved in diverse aspects of biotic and abiotic stresses, especially detoxification processes. Whether they regulate plant development remains unclear. Here, we report on our isolation by reverse transcription-polymerase chain reaction of a plant GST, AtGSTU17, from Arabidopsis (Arabidopsis thaliana) and demonstrate that.

    Glutathione S-Transferase. Cite this entry as: () Glutathione Transferases. In: Schwab M. (eds) Encyclopedia of Cancer.   Glutathione transferases (GSTs) are fundamental enzymes of the cell detoxification system. They catalyze the nucleophilic attack of glutathione (GSH) on electrophilic substrates to produce less toxic compounds. The resulting substrate can then be recognized by ATP-dependent transmembrane pumps and consequently expelled from the cell. Despite all the existing studies on .

    Qualitative and quantitative changes in glutathione S‐transferase (GSH‐T) were studied in human hepatocellular carcinoma. GSH‐T specific activity (/imoles per min per mg protein) was variably reduced in hepatocellular carcinoma. Similar changes were seen in “cationic” GSH‐T (ligandin) concentration determined by radioimmunoassay. Human cytosolic glutathione transferases: structure, function, and drug discovery Baojian Wu1 and Dong Dong2 1Division ofPharmaceutics, College Pharmacy, Jinan University, Huangpu Avenue West, Guangzhou, Guangdong 2 , China Department.


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Exploring the Functional Plasticity of Human Glutathione Transferases by Ann-Sofie Johansson Download PDF EPUB FB2

Exploring the Functional Plasticity of Human Glutathione Transferases: Allelic Variants, Novel Isoenzyme and Enzyme Redesign Article January with 2 Reads How we measure 'reads'Author: Ann-Sofie Johansson.

Structure and Function of Glutathione S-Transferases provides some of the latest information available on a variety of structural and functional components of glutathione S-transferases, a family of isozymes involved in many endogenous and exogenous functions in by: Exploring the Functional Plasticity of Human Glutathione Transferases: Allelic Variants, Novel Isoenzyme and Enzyme Redesign Glutathione transferases (GSTs) make up a superfamily that is involved in the cellular defense against various reactive compounds by catalyzing the conjugation of glutathione to electrophilic centra.

Members of this Author: Ann-Sofie Johansson. Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification.

The GST family consists of three superfamilies: the cytosolic, mitochondrial, and microsomal BRENDA: BRENDA entry. Kinsland, in Comprehensive Natural Products II, Glutathione S-transferase. GST has been used as an affinity fusion since 89 In many cases, GST has also been shown to enhance the solubility of the protein to which it is fused.

GST was one of the first widely adopted fusion tags for affinity purification and it has been used for the purification of innumerable proteins. Federici, L. et al. Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazolylthio)hexanol to human glutathione s-transferases Cited by: Open this publication in new window or tab >> Exploring the Functional Plasticity of Human Glutathione Transferases: Allelic Variants, Novel Isoenzyme and Enzyme Redesign Johansson, Ann-Sofie Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of.

Glutathione-S-transferases (GSTs) are a family of Phase II detoxification enzymes that catalyse the conjugation of glutathione (GSH) to a wide variety of. Johansson, A.-S., Exploring the Functional Plasticity of Human Glutathione Transferases. Allelic Variants, Novel Isoenzyme and Enzyme Redesign.

Acta Universitatis Upsaliensis Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 56 pp. Uppsala. ISBN   Johansson, A. Exploring the functional plasticity of human glutathione transferases: Allelic variants, novel ısoenzyme and enzyme releasing.

Acta universitatis upsaliensis (Comprehensive summaries of Uppsala dissertations from faculty of science and technology). Uppsala Google Scholar. This example demonstrates the functional plasticity of the glutathione transferase scaffold as well as the potential of rational active-site directed mutagenesis as a complement to DNA shuffling and other stochastic methods for the redesign of proteins with novel functions.

Place, publisher, year, edition, pages Vol.p. Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities Henri Pegeot1, Sandrine Mathiot2, Thomas Perrot1,Frederic Gense2, Arnaud Hecker1, Claude Didierjean2 and Nicolas Rouhier1 1 UMR Interactions Arbres/Microorganismes, Faculte des Sciences et Technologies, Universite de Lorraine/INRA.

Philip G. Board, Functional Genomics of the Human Glutathione Transferases, Encyclopedia of Drug Metabolism and Interactions, (), (). Wiley Online Library Allan W. Wolkoff and Paul D. Berk, Bilirubin Metabolism and Jaundice, Schiff's Diseases of the Liver, (), (). The 55 Arabidopsis glutathione transferases (GSTs) are, with one microsomal exception, a monophyletic group of soluble enzymes that can be divided into phi, tau, theta, zeta, lambda, dehydroascorbate reductase (DHAR) and TCHQD classes.

The populous phi and tau classes are often highly stress inducible and regularly crop up in proteomic and transcriptomic studies. Despite much.

Glutathione transferases (EC ) catalyze glutathione conjugation to electrophilic compounds, primarily produced from exogenous xenobiotics by biotransformation but which can also arise from endogenous substances.

The glutathione conjugation reaction is the first step of the mercapturic acid pathway, which is one of the most important detoxication processes (Fig. Purchase Glutathione Transferases and gamma-Glutamyl Transpeptidases, Volume - 1st Edition.

Print Book & E-Book. ISBNStockman PK, Beckett GJ, Hayes JD. Identification of a basic hybrid glutathione S-transferase from human liver. Glutathione S-transferase delta is composed of two distinct subunits (B1 and B2). Biochem J. Apr 15; (2)– [PMC free article] Hiley C, Fryer A, Bell J, Hume R, Strange RC.

The human glutathione S-transferases. C.-P.D. Tu's 48 research works with 2, citations and reads, including: Rat glutathione S-transferase M An isoenzyme with unique structural features including a redox-reactive cysteine.

This unit describes how pGEX vectors can be used in bacterial systems to express foreign polypeptides as fusions with glutathione‐S‐transferase (GST).In general, such fusion proteins are soluble and are easily purified from lysed cells under nondenaturing conditions by absorption with glutathione‐agarose beads, followed by elution in the presence of free glutathione.

Arabidopsis Book. ;8:e doi: /tab Epub May 8. Glutathione transferases. Dixon DP, Edwards R. The 55 Arabidopsis glutathione transferases (GSTs) are, with one microsomal exception, a monophyletic group of soluble enzymes that can be divided into phi, tau, theta, zeta, lambda, dehydroascorbate reductase (DHAR) and TCHQD classes.

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed).

Participates in the formation of novel hepoxilin regioisomers (PubMed). Regulates negatively CDK5 activity via p25/p35 translocation to prevent.Glutathione S -transferases (GSTs) traditionally have been studied in plants and other organisms for their ability to detoxify chemically diverse herbicides and other toxic organic compounds.

Anthocyanins are among the few endogenous substrates of plant GSTs that have been identified. The Bronze2 (Bz2) gene encodes a type III GST and performs the last genetically defined step of the maize.

Glutathione S-Transferases: Structure, Function and Clinical Implications: Medicine & Health Science Books @