Behavior of Acetyl Groups Combined with Sulfhydryl Groups in Protein:I. Acetylation of Sulfhydryl Groups in Yeast Alcohol Dehydrogenase

スポンサーリンク

概要

• 論文の詳細を見る

• It was found that highly purified crystalline yeast alcohol dehydrogenase (YADH) was still contaminated with a small amount of thiolesterase. Separation of these two enzymes from each other was performed by DEAE-cellulose column chromatography. YADH preparation resulted from this treatment was found to be homogeneous by disc electrophoresis and chromatography on hydroxylapatite column.Treatment of pure YADH with O, S-diacetylthiamine (DAT) in 0.05M phosphate buffer at pH 6.0 and 30° resulted in 50% inactivation of the enzyme with concomitant loss of two SH groups per mole of the protein. Reaction of the DAT-inactivated YADH with hydroxylamine resulted in full reactivation accompanied by restoration of SH groups to the level of the native enzyme.These results supply evidence that the change in enzymatic activity that occurs upon treatment of YADH with DAT is the consequence of acetylation of two SH groups essential for activity per molecule of the enzyme.

• 日本ビタミン学会の論文

著者

• 上原 喜八郎

  Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University

• 米沢 司郎

  Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University

• 梅本 準治

  Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University

• 大久保 修司

  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

• 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
• Inactivation of Yeast Alcohol Dehydrogenase by Dehydroascorbic Acid and D-Arabinosone
• 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

スポンサーリンク