Partial purification and some properties of human erythrocyte prostaglandin 9-ketoreductase and 15-hydroxyprostaglandin dehydrogenase. |
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Authors: | L Kaplan S C Lee L Levine |
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Affiliation: | Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02154 USA |
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Abstract: | Human erythrocytes were found to contain two prostaglandin metabolizing enzymes: a prostaglandin E 9-ketoreductase catalyzing the reduction of prostaglandin E2 to form prostaglandin F2α and a 15-hydroxyprostaglandin dehydrogenase that catalyzes the oxidation of prostaglandin F2α to form 15-ketoprostaglandin F2α. Both enzymes are found in the cytoplasmic fraction of erythrocytes and both enzymes use the triphosphopyridine nucleotides as cofactors more effectively than the diphosphopyridine nucleotides. These two enzymes were partially purified from erythrocyte homogenates and some of their properties were studied. |
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