Isolation and properties of enzymes involved in prostaglandin biosynthesis.
Prostaglandin (PG) endoperoxide synthetase was purified until homogeneity had been attained. The pure enzyme displays both cyclooxygenase and peroxidase activity, in accordance with the work of MIYAMOTO et al. (J. biol. Chem. 252, 2629--2636 (1976)). This enzyme therefore converts arachidonic acid into PGH2. Glutathione S-transferases, in the presence of glutathione, convert PGH2 into a mixture of PGF2alpha, PGE2 and PGD2. A new transferase in sheep lung gives mainly PGF2alpha and PGD2. Isolation and properties of these enzymes will be discussed. Finally, progress will be reported on the isolation of a soluble enzyme from various rat organs such as lung and spleen, which forms almost exclusively prostaglandin D.
D000818:Animals; D002417:Cattle; D005982:Glutathione Transferase / Q000302:isolation & purification* / Q000378:metabolism; D006168:Guinea Pigs; D006801:Humans; D008861:Microsomes / Q000201:enzymology; D010544:Peroxidases / Q000378:metabolism; D011451:Prostaglandin-Endoperoxide Synthases / Q000302:isolation & purification* / Q000378:metabolism; D011453:Prostaglandins / Q000096:biosynthesis*; D011817:Rabbits; D051381:Rats; D012710:Serum Albumin, Bovine; D012756:Sheep; D013045:Species Specificity; D013552:Swine
D011453:Prostaglandins; D012710:Serum Albumin, Bovine; D010544:Peroxidases; D011451:Prostaglandin-Endoperoxide Synthases; D005982:Glutathione Transferase