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Registro Completo |
Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
Data corrente: |
01/08/1992 |
Data da última atualização: |
11/12/2023 |
Autoria: |
PAGELS, W. R.; SACHS, R. J.; MARNETT, L. J.; DEWITT, D. L.; DAY, J. S.; SMITH, W. L. |
Título: |
Immunochemical evidence for the involvement of prostaglandin H synthase in hydroperoxide-dependent oxidations by ram seminal vesicle microsomes. |
Ano de publicação: |
1983 |
Fonte/Imprenta: |
The Journal of Biological Chemistry, v. 258, n. 10, p. 6517-6523, 1983. |
Idioma: |
Inglês |
Conteúdo: |
Abstract: Monoclonal antibodies against prostaglandin H (PGH) synthase have been used to precipitate cyclooxygenase and peroxidase activities from detergent-solubilized preparations of ram seminal vesicle microsomes. Approximately 85% of the solubilized cyclooxygenase activity was precipitated using an excess of anti-PGH synthase antibody; under similar conditions, immunoprecipitation of 60% of the diphenylisobenzofuran peroxidase, 75% of the phenylbutazone peroxidase, and 50% of the epinephrine peroxidase activities occurred. In contrast, less than 10% of the cyclooxygenase or peroxidase activities could be precipitated with nonimmune, control antibody preparations. These data indicate that the hydroperoxidase activity of PGH synthase is the major peroxidase activity catalyzing the co-oxidation of xenobiotics in ram seminal vesicle microsomes. |
Palavras-Chave: |
Prostaglandin-Endoperoxide Synthases. |
Thesagro: |
Endocrinologia; Ovino; Reprodução; Staphylococcus Aureus. |
Thesaurus Nal: |
Antibodies; Benzofurans; Endocrinology; Enzymology; Epinephrine; Hydrogen peroxide; Males; Microsomes; Phenylbutazone; Reproduction; Seminal vesicles; Sheep. |
Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
Marc: |
LEADER 01975naa a2200385 a 4500 001 1520203 005 2023-12-11 008 1983 bl uuuu u00u1 u #d 100 1 $aPAGELS, W. R. 245 $aImmunochemical evidence for the involvement of prostaglandin H synthase in hydroperoxide-dependent oxidations by ram seminal vesicle microsomes.$h[electronic resource] 260 $c1983 520 $aAbstract: Monoclonal antibodies against prostaglandin H (PGH) synthase have been used to precipitate cyclooxygenase and peroxidase activities from detergent-solubilized preparations of ram seminal vesicle microsomes. Approximately 85% of the solubilized cyclooxygenase activity was precipitated using an excess of anti-PGH synthase antibody; under similar conditions, immunoprecipitation of 60% of the diphenylisobenzofuran peroxidase, 75% of the phenylbutazone peroxidase, and 50% of the epinephrine peroxidase activities occurred. In contrast, less than 10% of the cyclooxygenase or peroxidase activities could be precipitated with nonimmune, control antibody preparations. These data indicate that the hydroperoxidase activity of PGH synthase is the major peroxidase activity catalyzing the co-oxidation of xenobiotics in ram seminal vesicle microsomes. 650 $aAntibodies 650 $aBenzofurans 650 $aEndocrinology 650 $aEnzymology 650 $aEpinephrine 650 $aHydrogen peroxide 650 $aMales 650 $aMicrosomes 650 $aPhenylbutazone 650 $aReproduction 650 $aSeminal vesicles 650 $aSheep 650 $aEndocrinologia 650 $aOvino 650 $aReprodução 650 $aStaphylococcus Aureus 653 $aProstaglandin-Endoperoxide Synthases 700 1 $aSACHS, R. J. 700 1 $aMARNETT, L. J. 700 1 $aDEWITT, D. L. 700 1 $aDAY, J. S. 700 1 $aSMITH, W. L. 773 $tThe Journal of Biological Chemistry$gv. 258, n. 10, p. 6517-6523, 1983.
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