Immobilization of catalytically active thromboxane synthase.
Thromboxane synthase has been immobilized on phenyl-Sepharose beads by adsorption. The immobilized enzyme is catalytically active and has a slightly lower apparent Km for PGH2 than the detergent-solubilized enzyme. However, both imidazole- and pyridine-based inhibitors are equally effective in inhibiting the immobilized and solubilized enzyme preparations. Although the immobilized enzyme appears to be less stable than the solubilized enzyme it is sufficiently stable to be used as a model for studying the properties of the enzyme.
Hall
E R
ER
Department of Internal Medicine, University of Texas Medical School, Houston 77030.
Townsend
G L
GL
Tuan
W M
WM
Venton
D L
DL
D000818:Animals; D002384:Catalysis; D002417:Cattle; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005231:Fatty Acids, Unsaturated / Q000096:biosynthesis; D008168:Lung / Q000201:enzymology; D011450:Prostaglandin Endoperoxides, Synthetic / Q000096:biosynthesis; D044262:Prostaglandin H2; D011463:Prostaglandins H / Q000096:biosynthesis; D012685:Sepharose; D013930:Thromboxane-A Synthase / Q000378:metabolism*
D004800:Enzymes, Immobilized; D005231:Fatty Acids, Unsaturated; D011450:Prostaglandin Endoperoxides, Synthetic; D011463:Prostaglandins H; D044262:Prostaglandin H2; C008033:12-hydroxy-5,8,10-heptadecatrienoic acid; D012685:Sepharose; D013930:Thromboxane-A Synthase