A1272-Anti-GOT1 Antibody

Total Page:16

File Type:pdf, Size:1020Kb

A1272-Anti-GOT1 Antibody BioVision 11/16 For research use only Anti-GOT1 Antibody CATALOG NO: A1272-100 ALTERNATIVE NAMES: Aspartate aminotransferase cytoplasmic; cAspAT; Cysteine aminotransferase cytoplasmic; Cysteine transaminase cytoplasmic; cCAT; Glutamate oxaloacetate transaminase 1; Transaminase A AMOUNT: 100 µl Western blot analysis of GOT1 IMMUNOGEN: KLH-conjugated synthetic peptide encompassing a sequence expression in Jurkat (A), A549 (B), within the center region of human GOT1 PC12 (C), H9C2 (D) whole cell lysates. HOST/ISOTYPE: Rabbit IgG CLONALITY: Polyclonal SPECIFICITY: Recognizes endogenous levels of GOT1 protein SPECIES REACTIVITY: Human and Rat PURIFICATION: The antibody was purified by affinity chromatography FORM: Liquid FORMULATION: Supplied in 0.42% Potassium phosphate; 0.87% Sodium chloride; pH 7.3; 30% glycerol and 0.01% sodium azide STORAGE CONDITIONS: Shipped at 4°C. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles DESCRIPTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as RELATED PRODUCTS: a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L- GOT2, human recombinant (Cat. No. 7809-100) cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is Aspartate Aminotransferase (AST or SGOT) Assay Kit (Cat. No. K753-100) converted into H2S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. FOR RESEARCH USE ONLY! Not to be used on humans. APPLICATION: WB; 1:500 – 1:1000 Note: This information is only intended as a guide. The optimal dilutions must be determined by the user. BioVision Incorporated Tel: 408-493-1800 | Fax: 408-493-1801 155 S. Milpitas Boulevard, Milpitas, CA 95035 USA www.biovision.com | [email protected] .
Recommended publications
  • AST / Aspartate Transaminase Assay Kit (ARG81297)
    Product datasheet [email protected] ARG81297 Package: 100 tests AST / Aspartate Transaminase Assay Kit Store at: -20°C Summary Product Description ARG81297 AST / Aspartate Transaminase Assay Kit is a detection kit for the quantification of AST / Aspartate Transaminase in serum and plasma. Tested Reactivity Hu, Ms, Rat, Mamm Tested Application FuncSt Specificity Aspartate aminotransferase (ASAT/AAT) facilitates the conversion of aspartate and alpha-ketoglutarate to oxaloacetate and glutamate. And then oxaloacetate and NADH are converted to malate and NAD by malate dehydrogenase. Therefore, the decrease in NADH absorbance at 340 nm is proportionate to AST activity. Target Name AST / Aspartate Transaminase Conjugation Note Read at 340 nm. Sensitivity 2 U/l Detection Range 2 - 100 U/l Sample Type Serum and plasma. Sample Volume 20 µl Alternate Names Cysteine transaminase, cytoplasmic; cAspAT; GIG18; Glutamate oxaloacetate transaminase 1; cCAT; EC 2.6.1.3; Cysteine aminotransferase, cytoplasmic; ASTQTL1; AST1; EC 2.6.1.1; Transaminase A; Aspartate aminotransferase, cytoplasmic Application Instructions Application Note Please note that this kit does not include a microplate. Assay Time 10 min Properties Form Liquid Storage instruction Store the kit at -20°C. Do not expose test reagents to heat, sun or strong light during storage and usage. Please refer to the product user manual for detail temperatures of the components. Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol GOT1 Gene Full Name glutamic-oxaloacetic transaminase 1, soluble Background Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, respectively.
    [Show full text]
  • Como As Enzimas Agem?
    O que são enzimas? Catalizadores biológicos - Aceleram reações químicas específicas sem a formação de produtos colaterais PRODUTO SUBSTRATO COMPLEXO SITIO ATIVO ENZIMA SUBSTRATO Características das enzimas 1 - Grande maioria das enzimas são proteínas (algumas moléculas de RNA tem atividade catalítica) 2 - Funcionam em soluções aquosas diluídas, em condições muito suaves de temperatura e pH (mM, pH neutro, 25 a 37oC) Pepsina estômago – pH 2 Enzimas de organismos hipertermófilos (crescem em ambientes quentes) atuam a 95oC 3 - Apresentam alto grau de especificidade por seus reagentes (substratos) Molécula que se liga ao sítio ativo Região da enzima e que vai sofrer onde ocorre a a ação da reação = sítio ativo enzima = substrato 4 - Peso molecular: varia de 12.000 à 1 milhão daltons (Da), são portanto muito grandes quando comparadas ao substrato. 5 - A atividade catalítica das Enzimas depende da integridade de sua conformação protéica nativa – local de atividade catalítica (sitio ativo) Sítio ativo e toda a molécula proporciona um ambiente adequado para ocorrer a reação química desejada sobre o substrato A atividade de algumas enzimas podem depender de outros componentes não proteicos Enzima ativa = Holoenzimas Parte protéica das enzimas + cofator Apoenzima ou apoproteína •Íon inorgânico •Molécula complexa (coenzima) Covalentemente ligados à apoenzima GRUPO PROSTÉTICO COFATORES Elemento com ação complementar ao sitio ativo as enzimas que auxiliam na formação de um ambiente ideal para ocorrer a reação química ou participam diretamente dela
    [Show full text]
  • Proceedings of the 1St Sino-German Workshop on Aspects of Sulfur Nutrition of Plants 23 - 27 May 2004 in Shenyang, China
    Institute of Plant Nutrition and Soil Science Ewald Schnug Luit J. de Kok (Eds.) Proceedings of the 1st Sino-German Workshop on Aspects of Sulfur Nutrition of Plants 23 - 27 May 2004 in Shenyang, China Published as: Landbauforschung Völkenrode Sonderheft 283 Braunschweig Federal Agricultural Research Centre (FAL) 2005 Sonderheft 283 Special Issue Proceedings of the 1st Sino-German Workshop on Aspects of Sulfur Nutrition of Plants 23 - 27 May 2004 in Shenyang, China edited by Luit J. De Kok and Ewald Schnug Bibliographic information published by Die Deutsche Bibliothek Die Deutsche Bibliothek lists this publication in the Deutsche Nationalbibliografie; detailed bibliographic data is available in the Internet at http://dnb.ddb.de . Die Verantwortung für die Inhalte der einzelnen Beiträge liegt bei den jeweiligen Verfassern bzw. Verfasserinnen. 2005 Landbauforschung Völkenrode - FAL Agricultural Research Bundesforschungsanstalt für Landwirtschaft (FAL) Bundesallee 50, 38116 Braunschweig, Germany [email protected] Preis / Price: 11 € ISSN 0376-0723 ISBN 3-86576-007-4 Table of contents Aspects of sulfur nutrition of plants; evaluation of China's current, future and available resources to correct plant nutrient sulfur deficiencies – report of the first Sino-German Sulfur Workshop Ewald Schnug, Lanzhu Ji and Jianming Zhou 1 Pathways of plant sulfur uptake and metabolism – an overview Luit J. De Kok, Ana Castro, Mark Durenkamp, Aleksandra Koralewska, Freek S. Posthumus, C. Elisabeth E. Stuiver, Liping Yang and Ineke Stulen 5 Advances in
    [Show full text]
  • Orphan Enzymes Could Be an Unexplored Reservoir of New Drug Targets
    Drug Discovery Today Volume 11, Numbers 7/8 April 2006 REVIEWS Reviews GENE TO SCREEN Orphan enzymes could be an unexplored reservoir of new drug targets Olivier Lespinet and Bernard Labedan Institut de Ge´ne´tique et Microbiologie, CNRS UMR 8621, Universite´ Paris Sud, Baˆtiment 400, 91405 Orsay Cedex, France Despite the immense progress of genomics, and the current availability of several hundreds of thousands of amino acid sequences, >39% of well-defined enzyme activities (as represented by enzyme commission, EC, numbers) are not associated with any sequence. There is an urgent need to explore the 1525 orphan enzymes (enzymes having EC numbers without an associated sequence) to bridge the wide gap that separates knowledge of biochemical function and sequence information. Strikingly, orphan enzymes can even be found among enzymatic activities successfully used as drug targets. Here, knowledge of sequence would help to develop molecular-targeted therapies, suppressing many drug-related side-effects. Biology is exploring numerous and diverse fields, each of which discovered before, despite intensive research by thousands of is very complex and difficult to study in its entirety. For many people studying the genetics and biochemistry of Saccharomyces years, immense advances in disclosing molecular functions have cerevisiae over the past 50 years. This observation has been con- been made using reductionist approaches, such as molecular firmed repeatedly, with the cohort of genomes that have been biology. Combining genetic, biophysical and biochemical con- sequenced, at a steady pace, over the past ten years. We now know cepts and methodologies has helped to disclose details of com- that many genes have been missed by reductionist approaches plex molecular mechanisms such as DNA replication.
    [Show full text]
  • Cystathionine-Β-Synthase: Molecular Regulation and Pharmacological Inhibition
    biomolecules Review Cystathionine-β-synthase: Molecular Regulation and Pharmacological Inhibition Karim Zuhra 1 , Fiona Augsburger 1 , Tomas Majtan 2 and Csaba Szabo 1,* 1 Chair of Pharmacology, Section of Medicine, University of Fribourg, 1702 Fribourg, Switzerland; [email protected] (K.Z.); fi[email protected] (F.A.) 2 Department of Pediatrics, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA; [email protected] * Correspondence: [email protected] Received: 14 April 2020; Accepted: 27 April 2020; Published: 30 April 2020 Abstract: Cystathionine-β-synthase (CBS), the first (and rate-limiting) enzyme in the transsulfuration pathway, is an important mammalian enzyme in health and disease. Its biochemical functions under physiological conditions include the metabolism of homocysteine (a cytotoxic molecule and cardiovascular risk factor) and the generation of hydrogen sulfide (H2S), a gaseous biological mediator with multiple regulatory roles in the vascular, nervous, and immune system. CBS is up-regulated in several diseases, including Down syndrome and many forms of cancer; in these conditions, the preclinical data indicate that inhibition or inactivation of CBS exerts beneficial effects. This article overviews the current information on the expression, tissue distribution, physiological roles, and biochemistry of CBS, followed by a comprehensive overview of direct and indirect approaches to inhibit the enzyme. Among the small-molecule CBS inhibitors, the review highlights the specificity and selectivity problems related to many of the commonly used “CBS inhibitors” (e.g., aminooxyacetic acid) and provides a comprehensive review of their pharmacological actions under physiological conditions and in various disease models. Keywords: hydrogen sulfide; cancer; Down syndrome; pharmacology; homocysteine; cystathionine 1.
    [Show full text]
  • Cysteine Catabolism and Glucosinolate Turnover in Arabidopsis Thaliana
    Cysteine catabolism and glucosinolate turnover in Arabidopsis thaliana Von der Naturwissenschaftlichen Fakultät der Gottfried Wilhelm Leibniz Universität Hannover zur Erlangung des Grades Doktorin der Naturwissenschaften (Dr. rer. nat.) genehmigte Dissertation von Saskia Brandt geb. Höfler, M. Sc. 2018 Referent: Prof. Dr. rer. nat. Hans-Peter Braun Korreferent: Prof. Dr. rer. nat. Helge Küster Tag der Promotion: 14.02.2018 The following publications contributed to this thesis: 1. Höfler S., Lorenz C., Busch T., Brinkkötter M., Tohge T., Fernie A.R., Braun H.-P., and Hildebrandt T.M. (2016): Dealing with the sulfur part of cysteine: four enzymatic steps degrade L-cysteine to pyruvate and thiosulfate in Arabidopsis mitochondria. Physiologia Plantarum 157 (3): 255–399 2. Lorenz C., Brandt S., Borisjuk L., Rolletschek H., Heinzel N., Tohge T., Fernie A.R., Braun H.-P., Hildebrandt T.M. (in preparation): Amino acid metabolism and the role of ETHE1 in Arabidopsis thaliana seeds. 3. Brandt S., Fachinger S., Tohge T., Fernie A.R., Braun H.-P. and Hildebrandt T.M. (in preparation): Extended darkness induces internal turnover of glucosinolates in Arabidopsis leaves. I Abstract Sulfur is an important chemical element in plants. It is taken up in form of sulfate and assimilation takes place in the cytosol, mitochondria and chloroplasts. The result of this process is, among others, the amino acid cysteine and the secondary metabolite glucosinolate. Under abiotic stress conditions such as low light or extended darkness, the plant has to catabolize amino acids and other metabolites to gain nutrients and energy. Cysteine can be catabolized via three pathways to pyruvate and persulfide.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2012/0266329 A1 Mathur Et Al
    US 2012026.6329A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2012/0266329 A1 Mathur et al. (43) Pub. Date: Oct. 18, 2012 (54) NUCLEICACIDS AND PROTEINS AND CI2N 9/10 (2006.01) METHODS FOR MAKING AND USING THEMI CI2N 9/24 (2006.01) CI2N 9/02 (2006.01) (75) Inventors: Eric J. Mathur, Carlsbad, CA CI2N 9/06 (2006.01) (US); Cathy Chang, San Marcos, CI2P 2L/02 (2006.01) CA (US) CI2O I/04 (2006.01) CI2N 9/96 (2006.01) (73) Assignee: BP Corporation North America CI2N 5/82 (2006.01) Inc., Houston, TX (US) CI2N 15/53 (2006.01) CI2N IS/54 (2006.01) CI2N 15/57 2006.O1 (22) Filed: Feb. 20, 2012 CI2N IS/60 308: Related U.S. Application Data EN f :08: (62) Division of application No. 1 1/817,403, filed on May AOIH 5/00 (2006.01) 7, 2008, now Pat. No. 8,119,385, filed as application AOIH 5/10 (2006.01) No. PCT/US2006/007642 on Mar. 3, 2006. C07K I4/00 (2006.01) CI2N IS/II (2006.01) (60) Provisional application No. 60/658,984, filed on Mar. AOIH I/06 (2006.01) 4, 2005. CI2N 15/63 (2006.01) Publication Classification (52) U.S. Cl. ................... 800/293; 435/320.1; 435/252.3: 435/325; 435/254.11: 435/254.2:435/348; (51) Int. Cl. 435/419; 435/195; 435/196; 435/198: 435/233; CI2N 15/52 (2006.01) 435/201:435/232; 435/208; 435/227; 435/193; CI2N 15/85 (2006.01) 435/200; 435/189: 435/191: 435/69.1; 435/34; CI2N 5/86 (2006.01) 435/188:536/23.2; 435/468; 800/298; 800/320; CI2N 15/867 (2006.01) 800/317.2: 800/317.4: 800/320.3: 800/306; CI2N 5/864 (2006.01) 800/312 800/320.2: 800/317.3; 800/322; CI2N 5/8 (2006.01) 800/320.1; 530/350, 536/23.1: 800/278; 800/294 CI2N I/2 (2006.01) CI2N 5/10 (2006.01) (57) ABSTRACT CI2N L/15 (2006.01) CI2N I/19 (2006.01) The invention provides polypeptides, including enzymes, CI2N 9/14 (2006.01) structural proteins and binding proteins, polynucleotides CI2N 9/16 (2006.01) encoding these polypeptides, and methods of making and CI2N 9/20 (2006.01) using these polynucleotides and polypeptides.
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur Et Al
    US 20150240226A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur et al. (43) Pub. Date: Aug. 27, 2015 (54) NUCLEICACIDS AND PROTEINS AND CI2N 9/16 (2006.01) METHODS FOR MAKING AND USING THEMI CI2N 9/02 (2006.01) CI2N 9/78 (2006.01) (71) Applicant: BP Corporation North America Inc., CI2N 9/12 (2006.01) Naperville, IL (US) CI2N 9/24 (2006.01) CI2O 1/02 (2006.01) (72) Inventors: Eric J. Mathur, San Diego, CA (US); CI2N 9/42 (2006.01) Cathy Chang, San Marcos, CA (US) (52) U.S. Cl. CPC. CI2N 9/88 (2013.01); C12O 1/02 (2013.01); (21) Appl. No.: 14/630,006 CI2O I/04 (2013.01): CI2N 9/80 (2013.01); CI2N 9/241.1 (2013.01); C12N 9/0065 (22) Filed: Feb. 24, 2015 (2013.01); C12N 9/2437 (2013.01); C12N 9/14 Related U.S. Application Data (2013.01); C12N 9/16 (2013.01); C12N 9/0061 (2013.01); C12N 9/78 (2013.01); C12N 9/0071 (62) Division of application No. 13/400,365, filed on Feb. (2013.01); C12N 9/1241 (2013.01): CI2N 20, 2012, now Pat. No. 8,962,800, which is a division 9/2482 (2013.01); C07K 2/00 (2013.01); C12Y of application No. 1 1/817,403, filed on May 7, 2008, 305/01004 (2013.01); C12Y 1 1 1/01016 now Pat. No. 8,119,385, filed as application No. PCT/ (2013.01); C12Y302/01004 (2013.01); C12Y US2006/007642 on Mar. 3, 2006.
    [Show full text]
  • Formação De Ligação Covalente Transitória Entre O Substrato E a Enzima)
    O que são enzimas? Catalizadores biológicos - Aceleram reações químicas específicas sem a formação de produtos colaterais PRODUTO SUBSTRATO COMPLEXO SITIO ATIVO ENZIMA SUBSTRATO Características das enzimas 1 - Grande maioria das enzimas são proteínas (algumas moléculas de RNA tem atividade catalítica) 2 - Funcionam em soluções aquosas diluídas, em condições muito suaves de temperatura e pH (mM, pH neutro, 25 a 37oC) Pepsina estômago – pH 2 Enzimas de organismos hipertermófilos (crescem em ambientes quentes) atuam a 95oC 3 - Apresentam alto grau de especificidade por seus reagentes (substratos) Molécula que se liga ao sítio ativo Região da enzima e que vai sofrer onde ocorre a a ação da reação = sítio ativo enzima = substrato 4 - Peso molecular: varia de 12.000 à 1 milhão daltons (Da), são portanto muito grandes quando comparadas ao substrato. 5 - A atividade catalítica das Enzimas depende da integridade de sua conformação protéica nativa – local de atividade catalítica (sitio ativo) glicose catalase Tetrâmero – 60KDa ~ 500aa hexoquinase 98000 Da 920aa Sítio ativo e toda a molécula proporciona um ambiente adequado para ocorrer a reação química desejada sobre o substrato A atividade de algumas enzimas podem depender de outros componentes não proteicos Enzima ativa = Holoenzimas Parte protéica das enzimas + cofator Apoenzima ou apoproteína •Íon inorgânico •Molécula complexa (coenzima) Covalentemente ligados à apoenzima GRUPO PROSTÉTICO COFATORES Elemento com ação complementar ao sitio ativo as enzimas que auxiliam na formação de um ambiente
    [Show full text]
  • Use of a Lipid Rich Strain Reveals Mechanisms of Nitrogen Limitation and Carbon Partitioning in the Haptophyte Tisochrysis Lutea
    1 Algal Research Achimer December 2016, Volume 20 Pages 229-248 http://dx.doi.org/10.1016/j.algal.2016.10.017 http://archimer.ifremer.fr http://archimer.ifremer.fr/doc/00356/46702/ © 2016 Elsevier B.V. All rights reserved Use of a lipid rich strain reveals mechanisms of nitrogen limitation and carbon partitioning in the haptophyte Tisochrysis lutea Garnier Matthieu 1, *, Bougaran Gael 1, Pavlovic Marija 2, Berard Jean-Baptiste 1, Carrier Gregory 1, Charrier Aurelie 1, Le Grand Fabienne 3, Lukomska Ewa 1, Rouxel Catherine 1, Schreiber Nathalie 1, Cadoret Jean-Paul 1, Rogniaux Hélène 2, Saint-Jean Bruno 1 1 IFREMER, PBA, Rue de l'Ile d'Yeu, BP 21105, 44311 Nantes Cedex 03, France 2 INRA UR1268 BIA, rue de la Géraudière, BP71627, 44313 Nantes Cedex 03, France 3 CNRS, Univ Brest, IRD, Ifremer, LEMAR, IUEM, Place Nicolas Copernic, 29280 Plouzané, France * Corresponding author : Matthieu Garnier, email addresses : [email protected] ; [email protected] Abstract : Haptophytes are a diverse monophyletic group with a worldwide distribution, known to be significantly involved in global climate regulation in their role as a carbon sink. Because nitrogen is a major limiting macronutrient for phytoplankton in oceans and for cultures of microalgae, understanding the involvement of nitrogen availability in haptophyte carbon partitioning is of global and biotechnological importance. Here, we made an ecophysiological study coupled with comprehensive large scale proteomic analysis to examine differences of behavior in reaction to nitrogen availability changes between a wild type strain of Tisochrysis lutea (WTc1) and a mutant strain (2Xc1) known to accumulate more storage lipids.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 7.404,951 B2 Teichberg (45) Date of Patent: Jul
    US007.404951B2 (12) United States Patent (10) Patent No.: US 7.404,951 B2 Teichberg (45) Date of Patent: Jul. 29, 2008 (54) METHOD AND COMPOSITION FOR DiGiorgio et al. "Gabaergic Systems in Brain Regions of Glutamate PROTECTING NEURONAL TISSUE FROM Lesioned Rats', Italien Journal of Biochemistry, 34(1): 19-28, 1985. DAMAGE INDUCED BY ELEVATED p. 19, Line 15. GLUTAMATE LEVELS Engelhardt etal. “The Diagnostic Value of Enzyme Determination in Cerebrospinal Fluid'. Medizinische Klinik, München, 71 (17): 699 (75) Inventor: Vivian I. Teichberg, Savyon (IL) 702, 1976. p. 701. Andrae etal. “Pyruvate and Related O-Ketoacids ProtectMammalian (73) Assignee: Yeda Research And Development Co. Cells in Culture Against Hydrogen Peroxide-Induced Cytotoxicity'. Ltd., Rechovot (IL) Toxicology Letters, 28:93-98, 1985. Avramis et al. "A Randomized Comparison of Native Escherichia (*) Notice: Subject to any disclaimer, the term of this coli Asparaginase and Polyethelyne Glycol Conjugated patent is extended or adjusted under 35 Asparaginase for Treatment of Children With Newly Diagnosed U.S.C. 154(b) by 95 days. Standard-RiskAcute Lymphoblastic Leukemia: A Children's Cancer Group Study”. Blood,99(6): 1986-1994, 2002. (21) Appl. No.: 10/522,415 Cavallini et al. “The Protective Action of Pyruvate on Recovery of Ischemic Rat Heart: Comparison With Other Oxidizable Substrates'. (22) PCT Filed: Jul. 31, 2003 Journal of Molecular Cell Cardiology, 22: 143-154, 1990. Desagher et al. “Pyruvate Protects Neurons Against Hydrogen Per (86). PCT No.: PCT/LO3/OO634 oxide-Induced Toxicity'. The Journal of Neuroscience, 17(23): 9060-9067, 1997. S371 (c)(1), Gramsbergen et al. “Pyruvate Protects Against 3-Nitropropionic (2), (4) Date: Jan.
    [Show full text]