Sökning: "Human GST A1-1"

Visar resultat 1 - 5 av 8 avhandlingar innehållade orden Human GST A1-1.

  1. 1. A Novel Route for Construction of Multipurpose Receptors through Chemical Modification of Glutathione Transferases

    Detta är en avhandling från Institutionen för teknik och naturvetenskap

    Författare :Johan Viljanen; Bengt Harald Jonsson; Kerstin Broo; Sophia Hober; [2008]
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Human GST A1-1; site-specific covalent modification; tyrosine 9; lysine 216; methionine 208; multipurpose receptor; pattern recognition; protein purification; NATURAL SCIENCES Chemistry; NATURVETENSKAP Kemi;

    Sammanfattning : This thesis describes how the human Alpha class glutathione transferase (GST) A1-1 can be reprogrammed either to function as a multipurpose biosensor for detection of small molecule analytes, or as a handle providing for more efficient protein purification.A novel, user-friendly, and efficient method for site-specific introduction of functional groups into the active site of hGST A1-1 is the platform for these achievements. LÄS MER

  2. 2. Role of Multiple Glutathione Transferases in Bioactivation of Thiopurine Prodrugs Studies of Human Soluble Glutathione Transferases from Alpha, Kappa, Mu, Omega, Pi, Theta, and Zeta Classes

    Detta är en avhandling från Uppsala : Acta Universitatis Upsaliensis

    Författare :Birgitta I. Eklund; Bengt Mannervik; Mikael Widersten; Ralf Morgenstern; [2006]
    Nyckelord :Biochemistry; Glutathione Transferases; Thiopurines; Prodrug; Bioactivation; Screening Method; Chemotherapy; Functional plasticity; Modulated activity; Biokemi;

    Sammanfattning : A screening method was developed for identification of catalytically active enzymes in combinatorial cDNA libraries of mutated glutathione transferase (GST) derivatives expressed in E. coli. The method is based on spraying monochlorobimane (MCB) directly over bacterial colonies growing on agar. LÄS MER

  3. 3. Alpha-class glutathione transferases as steroid isomerases and scaffolds for protein redesign

    Detta är en avhandling från Uppsala : Acta Universitatis Upsaliensis

    Författare :Pär L. Pettersson; Roberta F. Colman; [2002]
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Biochemistry; Biokemi; NATURAL SCIENCES Chemistry Biochemistry; NATURVETENSKAP Kemi Biokemi; Biokemi; Biochemistry;

    Sammanfattning : The present work focuses on the glutathione transferase (GST) Alpha-class enzymes, their characteristics as steroid isomerases and structural plasticity as malleable scaffolds for protein design. The GSTs are a family of detoxication enzymes that appears to have a wider variety of additional functions. LÄS MER

  4. 4. Catalysis and Site-Specific Modification of Glutathione Transferases Enabled by Rational Design

    Detta är en avhandling från Institutionen för fysik, kemi och biologi

    Författare :Sofia Håkansson Hederos; Lars Baltzer; Kerstin Broo; [2005]
    Nyckelord :TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; Catalysis; Glutathione Transferases; Rational design; Protein design; Site-specific modification; thiolester hydrolysis; TECHNOLOGY Bioengineering Enzyme engineering; TEKNIKVETENSKAP Bioteknik Enzymteknik;

    Sammanfattning : This thesis describes the rational design of a novel enzyme, a thiolester hydrolase, derived from human glutathione transferase (GST) A1-1 by the introduction of a single histidine residue. The first section of the thesis describes the design and the determination of the reaction mechanism. LÄS MER

  5. 5. Redesign of substrate specificity of glutathione transferase and glutathione reductase : Enzyme engineering by directed mutagenesis, phage-display selection and DNA shuffling

    Detta är en avhandling från Uppsala : Acta Universitatis Upsaliensis

    Författare :Lars O. Hansson; [1999]
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Biochemistry; Biokemi; NATURAL SCIENCES Chemistry Biochemistry; NATURVETENSKAP Kemi Biokemi; biokemi; Biochemistry;

    Sammanfattning : Human glutathione transferase (GST) A1-1 was expressed in fusion with the phage gene IIIproduct and a library of phage-displayed GST mutants was constructed by randomization of fouractive-site residues. Variant GSTs were isolated by mechanism-based phage display selection, using an immobilized transition-state analog of a nucleophilic aromatic substitution (SNAr) reaction. LÄS MER