STUDIES ON D-TETROSE METABOLISM : II. AN ENZYME FROM BEEF LIVER CATALYZING DISMUTATION OF D-TETROSE

スポンサーリンク

概要

• 論文の詳細を見る

• 1. When D-erythrose was incubated with beef liver preparation, a distinct decrease in reducing power, measured by Willstätter-Schudel's method was observed.2. The enzyme has been prepared in a soluble form from beef liver and purified about thirty fold.3. The enzyme shows pH optima at 6.0 and 7.5. During the reaction little oxygen uptake, little carbon dioxide output and litle change of optical density at 340mμ were observed. The enzyme acts more effectively upon D-threose than upon D-erythrose, but has no activity on the following compounds: D-ribose, D-xylose, D-arabinose, D-lyxose, D-glucose, D-galactose, D-mannose.4. From the reaction mixture containing D-erythrose as the substrate, erythritol and D-erythronic acid were detected by paper chromatography. When D-threose was used as the substrate, the reaction products were D-threitol and D-threonic acid.5. By treatment with alumina Cγ gel, the partially purified preparation was fractionated into a supernatant component (A) and an adsorbable, sodium citrate-extractable component (B). A or B alone showed little or no activity. When these components were mixed, almost the full activity was recovered.6. When B was mixed with catalytic amounts of NAD, the activity was largely regained. NAD could not be replaced by NADP. A as well as B is heat labile and non-dialyzable. Therefore, A seems to be the bound form of NAD-like substance.7. On the basis of these results, it can be expected that dismutation of D-tetrose to the corresponding polyol and acid in the presence of NAD-like substance takes place by the action of liver enzyme.

著者

• 溝口 正

  Laboratory Of Biochemistry Faculty Of Pharmaceutical Sciences Osaka University

• 菅野 浩一

  Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University

• 上原 喜八郎

  Laboratory of Biochemistry, Faculty of Pharmaceutical Science, Osaka University

関連論文

• Responses of Glutathione-Related Enzymes in Isolated Rat Small Intestine to Fe^-EDTA-Mediated Oxidative Stress
• Inhibition of Bovine Leukocyte Thioltransferase by Anti-inflammatory Drugs and Anti-histaminic Drugs
• Separation of the Molecular Forms of Chicken Liver Cytosolic Aldehyde Reductase and Comparison with Mitochondrial Aldehyde Reductase(Biological)
• Partial Purification and Some Properties of Mitochondrial Aldehyde Reductases from Chicken Liver
• Modulation of Subcellular Particles of the Rat Small Intestine and Liver by Ebselen
• STUDIES ON D-TETROSE METABOLISM : II. AN ENZYME FROM BEEF LIVER CATALYZING DISMUTATION OF D-TETROSE
• Studies on D-Tetrose Metabolism:III. Further Studies on Enzymes from Beef Liver Involved in D-Tetrose Metabolism
• Studies on D-tetrose metabolism. V. Identification of protecting factor against cold inactivation of D-erythrulose reductase from beef liver.:V. IDENTIFICATION OF PROTECTING FACTOR AGAINST COLD INACTIVATION OF D-ERYTHRULOSE REDUCTASE FROM BEEF LIVER
• The Photodynamic Action of Riboflavin-Adenine System on Bacteria, Bacteriophages, Influenza Virus, and Shigella exneri Antiserum
• Effect of Adenine on the Riboflavin-sensitized Photoreaction:I. Effect of Adenine on the Photodynamic Inactivation of Yeast Alcohol Dehydrogenase in the Presence of Riboflavin
• Behavior of Acetyl Groups Combined with Sulfhydryl Groups in Protein:I. Acetylation of Sulfhydryl Groups in Yeast Alcohol Dehydrogenase
• PREPARATION OF D-RIBOSE FROM D-ERYTHROSE BY CYANOHYDRIN REACTION
• Photodynamic Mutagenic Activity of Riboflavin for Transforming Deoxyribonucleic Acid and Accelerative Effect of Adenine
• Behavior of Acetyl Groups Combined with Sulfhydryl Groups in Protein:II. Behavior of Acetyl Groups Combined with Sulfhydryl Groups in Yeast Alcohol Dehydrogenase

もっと見る 閉じる

スポンサーリンク