Purification and Characterization of Glutathione-Independent Denitration Enzyme of Organic Nitrate Esters in Rabbit Hepatic Cytosol
| Autor: | Tetsuo Satoh, Takuya Hirose, Kiyomi Fukushima, Toshio Suwa, Mayumi Tsukamoto, Naoyoshi Ogawa |
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| Rok vydání: | 1995 |
| Předmět: |
Pharmaceutical Science
In Vitro Techniques Substrate Specificity Gel permeation chromatography chemistry.chemical_compound Cytosol Cytochrome P-450 Enzyme System Affinity chromatography Nitrate Transferases Animals Pharmacology chemistry.chemical_classification Nitrates Molecular mass Proteins Substrate (chemistry) General Medicine Glutathione Metabolism Hydrogen-Ion Concentration Chromatography Ion Exchange Molecular Weight Enzyme Liver chemistry Biochemistry Ammonium Sulfate Chromatography Gel Electrophoresis Polyacrylamide Gel Rabbits |
| Zdroj: | Biological and Pharmaceutical Bulletin. 18:1352-1355 |
| ISSN: | 1347-5215 0918-6158 |
| Popis: | The enzyme responsible for glutathione (GSH)-independent denitration of organic nitrate esters was purified by gel chromatography, ion-exchange chromatography and affinity chromatography from rabbit hepatic cytosol. The enzyme showed a molecular mass of 175 kDa and consisted of three subunits of 59 kDa. The enzyme exerted its maximum activities at around pH 9, when isosorbide dinitrate (ISDN) was used as substrate. The enzyme possessed a low Km value (10(-6) M) for various organic nitrate esters. The present enzyme is likely to be involved in the denitration of organic nitrate esters in conjunction with known enzymes, GSH S-transferase (GST) and cytochrome P450. |
| Databáze: | OpenAIRE |
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