Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila

Cell-free preparations of Tetrahymena thermophila catalyze the direct desaturation of cholesterol to Δ7-dehydrocholesterol (provitamin D3). The activity was isolated in the microsomal fraction from Tetrahymena homogenates. Δ7-Desaturase activity was stimulated fivefold by the addition of 6 mM ATP. O...

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Detalles Bibliográficos
Autores principales:	Valcarce, G., Florin-Christensen, J., Nudel, C.
Formato:	JOUR
Materias:	adenosine triphosphate delta 7 cholesterol desaturase nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide phosphate protozoal protein reduced nicotinamide adenine dinucleotide reduced nicotinamide adenine dinucleotide phosphate unclassified drug cholesterol lathosterol delta 5 dehydrogenase lathosterol delta-5-dehydrogenase oxidoreductase article biotechnology biotransformation chemical reaction kinetics dairy industry enzyme activity enzyme isolation nonhuman Tetrahymena thermophila animal culture medium enzymology growth, development and aging isolation and purification metabolism microsome Ciliophora Protozoa Animals Cholesterol Culture Media Microsomes Oxidoreductases Oxidoreductases Acting on CH-CH Group Donors
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_01757598_v53_n5_p591_Valcarce
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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