Partial purification and characterization of prostaglandin A isomerase from rabbit serum. |
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Authors: | H Polet L Levine |
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Institution: | Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02154 USA |
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Abstract: | Prostaglandin A isomerase has been purified 120-fold from rabbit serum by the use of ammonium sulfate fractionation, isoelectric focusing, and Sephadex G-200 chromatography. The molecular weight of the enzyme was estimated to be 110,000 from the elution volume on Sephadex G-200. Prostaglandin A isomerase is a heterogeneous protein with respect to charge. This has been concluded from the spread of enzymatic activity over 1 pH unit after isoelectric focusing. The enzymatic activity is inhibited by N-ethylmaleimide but not by other sulfhydryl blocking agents. The Km was determined to be 5 × 10?5m. |
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