Santiago Grisolı́a

Generalitat Valenciana

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Vicente Felipo

Centro de Investigacion Principe Felipe

Marı́a-Dolores Miñana

Hospital General Universitario De Valencia

Erwin Knecht

Centro de Investigacion Principe Felipe

José Hernández-Yago

Valencia Catholic University Saint Vincent Martyr

Vicente Rubio

University of Chile

Consuelo Guerri

Universitat de València

José‐Enrique O’Connor

Universitat de València

Mercedes Costell

Universitat de València

D. Diederich

University of Kansas

Barbara K. Joyce

Colorado State University

Cooperative Institutions

University of Kansas Medical Center

Instituto Valenciano de Investigaciones Agrarias

Universitat de València

University of Kansas

Instituto de Biomedicina de Valencia

Consejo Superior de Investigaciones Científicas

Instituto de Salud Carlos III

Centro de Investigacion Principe Felipe

Policlinico Umberto I

Centro de Investigación Biomédica en Red

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Formation of active phosphoenzymes with the diphosphoglycerate-dependant phosphoglycerate mutases

Biochemical Journal (1972)

H.G. Britton Josep Carreras Santiago Grisolı́a

Research Article| July 01 1972 Formation of active phosphoenzymes with the diphosphoglycerate-dependant phosphoglycerate mutases H G Britton; H G Britton 1Department of Biochemistry and Molecular Biology and Department of Obstetrics, University of Kansas Medical Center, Kansas City, Kans. 66103, U.S.A. Search for other works by this author on: This Site PubMed Google Scholar J Carreras; J Carreras 1Department of Biochemistry and Molecular Biology and Department of Obstetrics, University of Kansas Medical Center, Kansas City, Kans. 66103, U.S.A. Search for other works by this author on: This Site PubMed Google Scholar S Grisolia S Grisolia 1Department of Biochemistry and Molecular Biology and Department of Obstetrics, University of Kansas Medical Center, Kansas City, Kans. 66103, U.S.A. Search for other works by this author on: This Site PubMed Google Scholar Author and article information Publisher: Portland Press Ltd © 1972 The Biochemical Society1972 Biochem J (1972) 128 (3): 100P. https://doi.org/10.1042/bj1280100Pa Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn Email Cite Icon Cite Get Permissions Citation H G Britton, J Carreras, S Grisolia; Formation of active phosphoenzymes with the diphosphoglycerate-dependant phosphoglycerate mutases. Biochem J 1 July 1972; 128 (3): 100P. doi: https://doi.org/10.1042/bj1280100Pa Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Journal Search Advanced Search This content is only available as a PDF. © 1972 The Biochemical Society1972 Article PDF first page preview Close Modal You do not currently have access to this content.

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10.1042/bj1280100pa

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Effects of prenatal and postnatal exposure of rats to alcohol: Changes in (Na+K+) ATPase

Pharmacology Biochemistry and Behavior (1982)

Consuelo Guerri Santiago Grisolı́a

Liquid diet

10.1016/0091-3057(82)90474-9

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Comparative Studies in vivo and in vitro of Rat-Liver Enzymes

European Journal of Biochemistry (1974)

Matilde Salinas Ruth Wallace Santiago Grisolı́a

The stability of a number of enzymes which have a very short half-life as assessed by measurements in vivo, namely ornithine decarboxylase, serine dehydratase, tyrosine aminotransferase and 5-aminolevulinate synthase, and the stability of enzymes with a moderate half-life i.e. glutamate dehydrogenase, alanine aminotransferase and lactate dehydrogenase, were studied in whole liver and in tissue fractions thereof. While in general the measurements in vitro are in agreement with the data obtained in vivo, indicating the power of the simple technique herein described, there was enough variation in stability to indicate that in addition to their intrinsic basic stability due to the particular genetically determined structure of the protein, environmental factors must play an important role in the half-life of these enzymes. For example, tyrosine aminotransferase and particularly serine dehydratase are less stable in the tissue than in the homogenate and supernatant fractions and consequently are less stable in vitro than in vivo. Lactate dehydrogenase and alanine amino-transferase are stable for as long as 18 h in the homogenate and supernatant; however alanine aminotransferase activity in tissues decreases after 6 h incubation. The half-life of inactivation in the homogenate for glutamate dehydrogenase is 3–4 h. Interestingly, the activity in the tissue increases up to 6 h, while with longer periods of incubation the bulk of the enzyme leaked out into the medium and remained constant for 24 h. Experiments with “washed-residue” fractions show that the enzyme is inactivated by cytosol components. No clear difference between inactivation in vitro before and after starvation, following a high-protein diet or after injection of inhibitors was found for any of the enzymes studied.

Alanine

Tyrosine aminotransferase

10.1111/j.1432-1033.1974.tb03494.x

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MITOCHONDRIAL PROTEIN DEGRADATION

Elsevier eBooks (1979)

Santiago Grisolı́a Erwin Knecht Javier Cervera Juan Pablo Rojas Hernández

Degradation

10.1016/b978-0-08-023177-8.50019-6

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Los trastornos oculares del espectro alcohólico fetal

Archivos de la Sociedad Española de Oftalmología (2019)

M.D. Pinazo-Durán E. Bendala-Tufanisco Santiago Grisolı́a

10.1016/j.oftal.2019.12.002

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Control of urea synthesis and ammonia utilization in protein deprivation and refeeding

Archives of Biochemistry and Biophysics (1991)

Vicente Felipo María‐Dolores Miñana Santiago Grisolı́a

10.1016/0003-9861(91)90371-o

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Prenatal Exposure of Rats to Ammonia Impairs NMDA Receptor Function and Affords Delayed Protection Against Ammonia Toxicity and Glutamate Neurotoxicity

Journal of Neuropathology & Experimental Neurology (1995)

María‐Dolores Miñana Goizane Marcaida Santiago Grisolı́a Vicente Pelipo

The aim of this work was to assess whether perinatal hyperammonemia impairs the function of NMDA receptors and whether this impairment affords protection against acute ammonia toxicity and glutamate and NMDA neurotoxicity. Rats were exposed to ammonia during the prenatal and lactation periods by feeding the female rats an ammonium-containing diet since day 1 of pregnancy. After weaning (at postnatal day 21), the pups were fed a normal diet with no ammonia added. This treatment resulted in a marked decrease of the growth rate of the animals, which was maintained even 1 month after normalization of ammonia levels. Rats exposed to ammonia were more resistant than controls to acute ammonia toxicity 13 days after feeding a normal diet but not at 3 months. Primary cultures of cerebellar neurons from hyperammonemic rats showed decreased binding of [3H]MK-801 and were remarkably more resistant than controls to glutamate and NMDA toxicities. Also, the increase in aspartate aminotransferase activity induced by low concentrations of NMDA was not produced in such cultures. These results indicate that exposure to ammonia during the prenatal and lactation periods results in long-lasting impairment of NMDA receptor function. This would be the reason for the delayed protection afforded by exposure to low ammonia levels against acute ammonia toxicity in animals and against glutamate and NMDA toxicity in neuronal cultures.

Neurotoxicity

Hyperammonemia

10.1097/00005072-199509000-00005

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CARBON DIOXIDE AND AMMONIA FIXATION IN THE BIOSYNTHESIS OF CITRULLINE

Journal of Biological Chemistry (1951)

Santiago Grisolı́a R. H. Burris Philip P. Cohen

Carbon fixation

Ammonia production

10.1016/s0021-9258(18)50967-4

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Citations (20)

Carbamyl transfer with mammalian and bacterial enzymic preparations

Biochimica et Biophysica Acta (1955)

Santiago Grisolı́a Donald P. Wallach Harold Grady

Carbamyl Phosphate

Ion chromatography

Specific activity

10.1016/0006-3002(55)90337-1

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Citations (17)

Biosynthesis and Utilization of Acetyl Phosphate, Formyl Phosphate, and Carbamyl Phosphate and their Relations to the Urea Cycle

Advances in chemistry series (1964)

Santiago Grisolı́a Luisa Raijman

Animal and bacterial enzymes that utilize or synthesize carbamyl phosphate have activity with acetyl phosphate. Acyl phosphatase hydrolyzes both substrates, and maybe involved in the specific dynamic action of proteins. Ornithine and aspartic transcarbamylases also synthesize acetylornithine and acetyl aspartate. Finally, bacterial carbamate kinase and animal carbamyl phosphate synthetase utilize acetyl phosphate as well as carbamyl phosphate in the synthesis of adenosine triphosphate. The synthesis of acetyl phosphate and of formyl phosphate by carbamyl phosphate synthetases is described. The mechanism of carbon dioxide activation by animal carbamyl phosphate synthetase is reviewed on the basis of the findings concerning acetate and formate activation.

Carbamyl Phosphate

Carbamoyl phosphate synthetase

10.1021/ba-1964-0044.ch010

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Citations (31)