Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Pierre M. Sinet"'
Autor:
Pierre M. Sinet, Yvon Lamour
This volume contains the proceedings of the meeting Genetics and Alzheimer's Disease held in Paris, on March 25,1988, by the Fondation Ipsen pour la Recherche Therapeuti que. This meeting was the second of the series of Colloques Medecine et Recher
Autor:
Irène Ceballos, France Javoy-Agid, Etienne C. Hirsch, Sylvie Dumas, Pierre P. Kamoun, Pierre M. Sinet, Yves Agid
Publikováno v:
Neuroscience Letters. 105:41-46
The cellular localization of copper-zinc superoxide dismutase (CuZn SOD) mRNA was determined in the human hippocampus by in situ hybridization with a 35S-labelled DNA probe complementary to human CuZn SOD mRNA. A positive hybridization signal was det
Publikováno v:
Biochemical Pharmacology. 31:521-525
Human red blood cells treated with the CuZn superoxide dismutase inhibitor diethyldithio-carbamate (DDC) undergo metabolic modifications in addition to the superoxide dismutase inhibition: oxidation of the reduced glutathione (GSH) to oxidized glutat
Publikováno v:
Journal of Neurochemistry. 34:1421-1428
H2 O2 production by rat brain in vivo was observed with a method based on the measurement of brain catalase. The administration to the rat of 3-amino-1, 2, 4-triazole, an H2 O2- dependent inhibitor of catalase, caused progressive inhibition of brain
Publikováno v:
Alcoholism: Clinical and Experimental Research. 4:366-370
Can brain metabolize ethanol? We present data demonstrating that brain catalase in conjunction with endogenous H2O2 will oxidize ethanol in vivo. The method is based on an H2O2-dependent inhibition of brain catalase in vivo by 3-amino-1,2,4-triazole
Autor:
Francis Galibert, Annie Nicole, Yves Jacob, Michèle Meunier-Rotival, Pierre-M. Sinet, Henri Jerome, Jean-Maurice Delabar, Luc d'Auriol
Publikováno v:
European Journal of Biochemistry. 166:181-187
The molecular cloning and nucleotide sequence of a cDNA clone (pR SOD) for rat CuZn superoxide dismutase (CuZnSOD) is reported. Nucleotide sequence homology with human superoxide dismutase is 86% for the coding region and 71% for the 3' untranslated
Publikováno v:
Biochemical and biophysical research communications. 129(1)
The activity of manganese superoxide dismutase (MnSOD) revealed by specific staining after gel electrophoresis of cell extracts, is decreased in human fibroblasts transformed by SV 40. The decrease in enzyme activity is attributable to decreased amou
Autor:
Pierre M. Sinet
Publikováno v:
Annals of the New York Academy of Sciences. 396
Autor:
Pierre-M. Sinet, Pascale Garber
Publikováno v:
Archives of biochemistry and biophysics. 212(2)
Human copper-zinc superoxide dismutase undergoes inactivation when exposed to O2− and H2O2 generated during the oxidation of acetaldehyde by xanthine oxidase at pH 7.4 and 37° C. In contrast, human manganese superoxide dismutase is not inactivated