Growth Factor Regulation of Prostaglandin H Synthase Gene Expression

Autor:	M. J. Bienkowski, R. R. Gorman, A. H. Lin
Rok vydání:	1991
Předmět:	chemistry.chemical_classification Protoporphyrin IX biology Chemistry Carbohydrate Trypsin Cofactor chemistry.chemical_compound Enzyme Biochemistry Gene expression medicine biology.protein Arachidonic acid GSK3B medicine.drug
Zdroj:	Eicosanoids and Other Bioactive Lipids in Cancer and Radiation Injury ISBN: 9781461367277
DOI:	10.1007/978-1-4615-3874-5_44
Popis:	Over the past 20 years, the prostaglandin H synthase (PGHS) (EC 1.14.99.1) has been one of the most heavily studied enzymes in lipid biochemistry (1–3). The purified enzyme is a homodimer of 70-kDa subunits that contain 3.5% carbohydrate of the high mannose type by weight (4–7). The enzyme contains an Fe3+ protoporphyrin IX prosthetic group and catalyzes both the bisdioxygenation of arachidonic acid to the hydroperoxyendoperoxide PGG2 and the reduction of PGG2 to the hydroxyendoperoxide PGH2. The apoprotein of PGHS can be readily cleaved by trypsin to form two protein fragments: a 33-kDa fragment that contains the amino terminus and a 38-kDa fragment that includes the carboxyl terminus and the aspirin-binding site.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::e39047246ec7012307b295776bfe4bd3 https://doi.org/10.1007/978-1-4615-3874-5_44 Zobrazit plný text záznamu