Prostaglandin D2-synthase from cattle brain: purification and physico-chemical properties

Prostaglandin D2-synthase has been purified from bovine brain for the first time and characterized. The enzyme has a molecular mass of 21 kDa and a pH optimum at 9.0 and is activated by dithiothreitol. The presence in the enzyme molecule of carbohydrates and lipids has been established and a prelimi...

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Bibliographic Details
Published in:	Biokhimiia (Moscow, Russia) Vol. 59; no. 2; p. 251
Main Authors:	Avakian, S A, Boiadzhian, A S, Pogosian, A G, Karagezian, K G
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-02-1994
Subjects:	Animals Brain - enzymology Cattle Chromatography, DEAE-Cellulose Chromatography, Gel Chromatography, Thin Layer Hydrogen-Ion Concentration Intramolecular Oxidoreductases Isomerases - isolation & purification Isomerases - metabolism Lipocalins Molecular Weight
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Summary:	Prostaglandin D2-synthase has been purified from bovine brain for the first time and characterized. The enzyme has a molecular mass of 21 kDa and a pH optimum at 9.0 and is activated by dithiothreitol. The presence in the enzyme molecule of carbohydrates and lipids has been established and a preliminary conclusion made about the qualitative composition of the lipids. The ability of the enzyme to form aggregates under the influence of the detergent has been demonstrated. The role of the lipid component in the preservation of the enzyme monomeric structure as well as the possible mechanisms of action of the above inhibitors and activators are discussed.
ISSN:	0320-9725