4 edition of Glutathione S-transferases found in the catalog.
Includes bibliographical references and index.
|Statement||edited by N.P.E. Vermeulen ...[et al.].|
|Contributions||Vermeulen, N. P. E.|
|LC Classifications||QP606.G59 G59 1996|
|The Physical Object|
|Pagination||xxv, 261 p.,  p. of plates :|
|Number of Pages||261|
|LC Control Number||96172984|
Glutathione is a simple sulfur compound composed of three amino acids and the major non-protein thiol in many organisms, including plants. The functions of glutathione are manifold but notably include redox-homeostatic buffering. Glutathione status is modulated by oxidants as well as by nutritional and other factors, and can influence protein structure and activity through changes in thiol. In this week's UltraWellness blog, Dr. Mark Hyman gives you the lowdown on the "mother of all antioxidants" and tells you how you can boost it in your body -- naturally. To find out more, visit.
Structure and Function of Glutathione S-Transferases - CRC Press Book 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 cells. Book Description. 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 cells.
Glutathione transferases are multifunctional enzymes. Some of the known functions of the enzymes are biotransformation of xenobiotics, countering oxidative stress and participating in cell regulatory functions. As the isoforms present in number of classes the purification of a particular isoform for characterization is a challenging task. In insect, the study of GSTs is focusing on their roles Cited by: 1. Cytosolic glutathione (GSH) transferases (GSTs) exist as stable homo- and heterodimers. Interactions at the subunit interface serve an important role in stabilizing the subunit tertiary structures of all GSH transferases. In addition, the dimer is required to maintain functional conformations at the active site on each subunit and the nonsubstrate ligand binding site at the dimer interface Cited by:
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William B. Coleman PhD, in Molecular Pathology (Second Edition), GSTP1. Glutathione S-transferases are enzymes responsible for the detoxification of reactive chemical species through conjugation to reduced glutathione.
The GSTP1 gene, encoding the pi class glutathione S-transferase, was the first hypermethylated gene to be characterized in prostate cancer . The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance Study on PubMed.
GST's on Wikipedia. On Amazon (a thorough book on GST's): Glutathione S-Transferases: Structure. Glutathione S-Transferases: Structure, Function and Clinical Implications: Medicine & Health Science Books @ hor: Gerard J. Mulder. 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 cells.
Molecular studies presented in the book focus on the regulation of these Cited by: The glutathione S-transferase (GST) gene family encodes genes that are critical for certain life processes, as well as for detoxication and toxification mechanisms, via conjugation of reduced glutathione (GSH) with numerous substrates such as pharmaceuticals and environmental GST genes are upregulated in response to oxidative stress and are inexplicably overexpressed in Cited by: Author: Kenneth D.
Tew,Cecil B. Pickett,Timothy J. Mantle,Bengt Mannervik; Publisher: CRC Press ISBN: Category: Medical Page: View: DOWNLOAD NOW» 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.
The Glutathione S-transferases (GSTs) form a group of multi-gene isoenzymes involved in the cellular detoxification of both xenobiotic and endobiotic compounds. GSTs have been divided into a.
A proteomic analysis identifies glutathione S-transferase isoforms whose abundance is differentially regulated by ethylene during the formation of early root epidermis in Arabidopsis seedlings.
Biochim. Biophys. Acta. ; 8 (1)– Marrs K.A. The functions and regulation of glutathione S-transferases in plants.
Annu. Rev. Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structural fold. Each monomer is composed of a distinct N-terminal sub-domain, which adopts the thioredoxin fold, and a C-terminal all-helical ro: IPR In Glutathione S-Transferases: Structure, Function and Clinical Implications, the most recent scientific developments in this enzyme system are presented and discussed.
The book covers the structure of GSTs, together with their role not only in susceptibility to cancer but also in cancer prevention. Find many great new & used options and get the best deals for Glutathione S-Transferases: Structure, Function and Clinical Implications by G.
Mulder, W. Peters, N. Vermeulen, P. Van Bladeren and H. Nieuwenhuyse (, Hardcover) at the best online. Glutathione S‐transferases. Philip J. Sherratt. University of Dundee, UK. Search for more papers by this author Book Editor(s): Costas Ioannides. School of Biomedical and Life Sciences, University of Surrey, Guildford, Surrey GU2 7XH, UK.
Search for more papers by this author the transport of hydrophobic ligands and glutathione. Sharad Singhal, Kenneth Drake, Sushma Yadav, Jyotsana Singhal and Sanjay Awasthi, Enzymology of Glutathione S-Transferases, Toxicology of Glutathione Transferases, /ch16, (), ().Cited by: The Glutathione S-Transferase (GST) AssayKit utilizes 1-Chloro-2,4-dinitrobenzene (CDNB) which is suitable for the broadest range of GST isozymes.
Upon conjugation of the thiol group of glutathione to the CDNB substrate, there is an increase in the absorbance at nm. The Glutathione S-Transferase (GST) File Size: KB.
Glutathione S-transferases (GSTs) are multifunctional enzymes involved in the metabolism of a broad variety of xenobiotics and endogenous compounds (e.g., antibiotics, steroids, prostaglandins.
Glutathione s-transferases (GSTs) constitute the most important enzymes protecting human and many other organisms from potentially toxic chemicals, including drugs and carcinogens.
This book reviews scientific developments in research of this enzyme. Glutathione s-transferases (GSTs) constitute the most important enzymes protecting human and many other organisms from potentially toxic chemicals, including drugs and carcinogens.
This book reviews scientific developments in research of this enzymePrice: $ Further contributions center on the diversified roles of different glutathione-S-transferases and the roles of nitrosoglutathione and glutaredoxins - a subfamily of redoxins.
The book closes with discussions of the analogous or homologous thiol metabolism in pathogens and the potential suitability of involved enzymes as drug targets. The major roles of glutathione (GSH) and glutathione S-transferases (GSTs) in the detoxification of xenobiotics predicts their important role in drug resistance.
As such, both GSH and GSTs have been manipulated as targets in the design of novel chemotherapeutic by: 2. Hayes JD, Kerr LA, Cronshaw AD () Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation.
Molecular relationships between the B1 and B2 subunits and other alpha class glutathione S-transferases. Biochem J –Cited by:. Part 1 Enzymology of the glutathione S-transferases, the glutathione S-transferases and their contribution to drug resistance in nature,t and ; rapid purification of glutathione S-tranferases by gradient affinity elution of the glutathione-agarose and the S-hexylglutathione-agarose chromatography matrics, J.D.
Glutathione S -transferases (GSTs) are ubiquitous enzymes that catalyze the conjugation of toxic xenobiotics and oxidatively produced compounds to reduced glutathione, which facilitates their metabolism, sequestration, or removal. We report here that soybean (Glycine max) root nodules contain at least 14 forms of GST, with GST9 being most prevalent, as measured by both real-time reverse.Glutathione S-transferases (EC ) are thought to play a physiological role in initiating the detoxication of poten- tial alkylating agents (l-3)) including pharmacologically active compounds.
These enzymes catalyze the reaction of such com- pounds (Fig. 1) with the -SH group of glutathione, thereby.