STUDIES ON BIOLOGICAL FUNCTIONS OF 5-METHYLTHIOADENOSINE VITAMIN B12-REPLACING EFFECT FOR OCHROMONAS MALHAMENSIS

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概要

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• An unidentified factor which can completely replace the vitamin B12 requirement of a protozoan, Ochromonas malhamensis, was found in commercial yeast extract powder. The factor showed a positive sugar test with orcinol reagent. The presence of sulfur was demonstrated with platinic iodide reagent. The molecular weight, 297, and the chemical formula, C11H15O3N5S, were determined by mass spectrometry and elemental analysis. Infra-red and nuclear magnetic resonance studies indicated the presence of a thiomethyl group. The factor was hydrolyzed by treatment with acid into adenine and 5-methylthioribose, i.e., the sugar constituent of 5-methylthioadenosine. The factor was identified as 5methylthioadenosine from the behavior exhibited in thin-layer chromatography and from microbiological tests for its vitamin B12-replacing effect.

• 財団法人 学会誌刊行センターの論文

著者

• 杉本 喜憲

  京大工 工業化学

• 杉本 喜憲

  Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, K

• 福井 三郎

  Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, K

• 杉本 喜憲

  Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, Kyoto University

• 福井 三郎

  Laboratory of Industrial Biochemistry, Deparmtnt of Industrial Chemistry, Faculty of Engineering, Kyoto University

関連論文

• 3.5′-メチルチオアデノシンの生物学的役割の研究 : Ochromonas malhamensisにおけるビタミンB_代替効果(JOURNAL OF NUTRITIONAL SCIENCE AND VITAMINOLOGY : 掲載論文要旨)
• Studies on biological functions of 5′-methylthioadenosine vitamin B12-replacing effect for Ochromonas malhamensis
• 3.OchromonasのビタミンB_12代替作用物質としての5'-Methylthioadenosineの固定(ビタミンB研究委員会 : 第212回会議研究発表要旨)
• 52.プロパンジオール脱水酵素のアポたん白に対する各種ビタミンB_体の結合性(研究発表)(日本ビタミン学会 : 第23回大会研究発表要旨)
• 15. ジオール脱水酵素とビタミンB_補酵素の結合と解離における金属イオンの役割(ビタミンB研究委員会第200回会議研究発表要旨)
• STUDIES ON BIOLOGICAL FUNCTIONS OF 5-METHYLTHIOADENOSINE VITAMIN B12-REPLACING EFFECT FOR OCHROMONAS MALHAMENSIS
• The Mechanism of in Situ Reactivation of Glycerol-Inactivated Coenzyme B12-Dependent Enzymes, Glycerol Dehydratase and Diol Dehydratase
• PYRIDOXAL PHOSPHATE N-OXIDE. ANALYSES OF COENZYMATIC ACTIVITIES FOR TRYPTOPHANASE AND ASPARTATE AMINOTRANSFERASE BY USE OF STOPPED FLOW METHOD
• BINDING OF PYRIDOXAL PHOSPHATE N-OXIDE TO MITOCHONDRIAL AND CYTOPLASMIC ASPARTATE AMINOTRANSFERASES AND SOME CHARACTERISTICS OF THE RESULTING ARTIFICIAL HOLOENZYMES
• INHIBITION OF ACTIVITIES OF ASPARTATE AMINO-TRANSFERASE AND TRYPTOPHANASE BY EXCESS BINDING OF PYRIDOXAL 5'-PHOSPHATE
• COENZYMATIC ACTIVITIES OF 2-NOR-2-HYDROXY-METHYL PYRIDOXAL 5'-PHOSPHATE FOR VARIOUS VITAMIN B6 ENZYMES
• TRANSFER OF PYRIDOXAL 5'-PHOSPHATE FROM ALBUMIN-PYRIDOXAL 5'-PHOSPHATE COMPLEX TO APO-ASPARTATE AMINOTRANSFERASE
• Spectrophotometric Demonstration of Vitamin B12S-Formation by Nucleophilic Cleavage of Co-C Bond of Acetylcobalamin
• STUDIES ON THE OXIDATION PRODUCTS OF LIPOIC ACID

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