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Prostaglandin endoperoxide synthase isozymes

1997
Abstract PGH synthases catalyze the initial reaction common to the formation of prostanoids and are the target sites for most nonsteroidal anti-inflammatory drugs (NSAIDs). Until the recent discovery of a second PGH synthase isozyme (PGH synthase-2; PGHS-2), it was thought that NSAIDs acted by inhibiting a single enzyme, now referred to as PGH ...
William L. Smith, David L. DeWitt
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Mechanism of Hydroperoxide Reduction by Mangano-Prostaglandin Endoperoxide Synthase

Biochemistry, 1996
Reaction of manganese-reconstituted prostaglandin endoperoxide synthase (Mn-PGHS) with 15-hydroperoxyeicosatetraenoic acid (15-HPETE) generates two products in nearly equal amounts: 15-hydroxyeicosatetraenoic acid (15-HETE) and 15-ketoeicosatetraenoic acid (15-KETE) [Kulmacz et al. (1994) Biochemistry 33, 5428-5439]. Their proposed mechanism to explain
L M, Landino, L J, Marnett
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Prostaglandin Endoperoxide H Synthases-1 and -2

1996
Publisher Summary The chapter compares and contrasts the structural and kinetic properties of prostaglandin endoperoxide H synthase-1 (PGHS-1) and -2. It also discusses the description of the interactions of the two isozymes with nonsteroidal anti-inflammatory drugs (NSAIDs). There are three general areas of study important to understanding more about
W L, Smith, D L, Dewitt
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Immunocytochemical localization of prostaglandin endoperoxide synthase in the bovine intestine

Histochemistry, 1993
The localization of prostaglandin (PG) endoperoxide synthase in bovine intestine was examined immunocytochemically with polyclonal antibody raised against PG endoperoxide synthase purified from bovine seminal glands. The most intense positive staining reaction for the enzyme was present in mast cells.
K, Ishimura   +6 more
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Inactivation of prostaglandin endoperoxide synthase by acylating derivatives of indomethacin

Biochemistry, 1993
Derivatives of the potent antiinflammatory agent and cyclooxygenase inhibitor indomethacin were synthesized in which the carboxylic acid moiety was converted into reactive acylating agents. Indomethacin imidazole (indomethacin-IM) and indomethacin N-hydroxysuccinimide (indomethacin-NHS) inactivated both the cyclooxygenase and peroxidase activities when
I, Wells, L J, Marnett
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Inhibition of lipoxygenase and prostaglandin endoperoxide synthase by anacardic acids

Biochemical and Biophysical Research Communications, 1991
C22:1 omega 5-anacardic acid was found to be a good inhibitor of both potato lipoxygenase and ovine prostaglandin endoperoxide synthase with approximate IC50's of 6 and 27 microM, respectively. Very similar inhibition was seen with the crude exudate, rich in omega 5-anacardic acids, from glandular trichomes of an arthropod-resistant strain of geranium,
R, Grazzini   +8 more
openaire   +2 more sources

Characterization of a Tyrosyl Radical in Prostaglandin Endoperoxide Synthase-2

Biochemical and Biophysical Research Communications, 1994
Two different isoforms of prostaglandin H synthase, prostaglandin H synthase-1 and prostaglandin H synthase-2, have been identified. Both isozymes catalyze both cyclooxygenase and peroxidase reactions. Residues identified as being essential for catalysis by ovine prostaglandin endoperoxide H synthase-1 are all conserved in prostaglandin H synthase-2 ...
L C, Hsi   +3 more
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Expression of prostaglandin endoperoxide synthase-1 in a baculovirus system

Biochemical and Biophysical Research Communications, 1992
A cDNA coding for ovine prostaglandin endoperoxide (PGH) synthase-1 was used to construct a recombinant baculovirus which was expressed in Spodoptera frugiperda (Sf9) insect cells. Two proteins reactive with anti-PGH synthase antibody were produced. A larger protein (Mr = 72,000) coelectrophoresed with native enzyme; a smaller, more abundant protein ...
T, Shimokawa, W L, Smith
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Localization of prostaglandin endoperoxide synthase in the human corpus luteum

Human Reproduction, 1990
Prostaglandins have been implicated in both maintenance and luteolysis of the primate corpus luteum. Central to the production of prostaglandins is the enzyme prostaglandin endoperoxide synthase (PGHS). In the present study, we identified the cell types which contain PGHS in 44 human corpora lutea, using immunoperoxidase staining techniques.
S W, Kauma   +3 more
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Not prostacyclin synthase but prostaglandin endoperoxide synthase increases with human placental development

Prostaglandins, 1986
Prostaglandin endoperoxide synthase (i.e. cyclooxygenase; PGH synthase) and prostacyclin synthase (PGI synthase) were quantitated with specific immunoradiometric assays in microsomes from human placentae (n = 20) obtained from 7 up to 17 weeks of gestation.
M J, Keirse, J J, Erwich, G, Klok
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