Formation of m-Tyrosine and o-Tyrosine from L-Phenylalanine by Rat Brain Homogenate
スポンサーリンク
概要
- 論文の詳細を見る
Incubation of L-phenylalanine with rat brain homogenate in the presence of a pteridine co-factor and 2-mercaptoethanol gave rise to three hydroxylated products which were identified with high-performance liquid chromatography as p-tyrosine, m-tyrosine and o-tyrosine.
- 公益社団法人日本薬学会の論文
- 1980-05-25
著者
-
石光 進
Kyoto Phramaceutical Univeristy
-
小原 晃
Kyoto College of Pharmacy
-
小原 晃
Laboratory Of Biochemistry Kyoto Pharmaceutical University
-
藤本 貞毅
Kyoto Pharmaceutical University
-
藤本 貞毅
Laboratory Of Biochemistry Kyoto Pharmaceutical University
関連論文
- Studies on the Active Site of Papain. III. Inhibition by Dibasic Acids
- Two Distinct Low-Molecular-Weight Acid Phosphatases from Rat Liver
- Inactivation of Cholinesterase by Ascorbic Acid in the Presence of Cupric Ions : A Possible Mechanism for the Inactivation of an Enzyme by the Metal-Catalyzed Oxidation System
- Nonenzymatic Glycation of Transferrin : Decrease of Iron-Binding Capacity and Increase of Oxygen Radical Production
- On the Mechanism of Inactivation of Active Papain by Ascorbic Acid in the Presence of Cupric Ions
- Hydroxylation of Phenylalanine and Salicylate by Stimulated Polymorphonuclear Leukocytes and the Accelerating Effect of Glutathione on Their Hydroxylation
- Effect of Radical Scavengers on the Inactivation of Papain by Ascorbic Acid in the Presence of Cupric Ions
- Purification and Characterization of Zinc-Dependent Acid Phosphatase from Bovine Brain
- Formation of a Hydroxyl Radical by the Myeloperoxidase-NADH-Oxygen System
- Site-Specific Inactivation of Papain by Ascorbic Acid in the Presence of Cupric Ions
- Characterization of Cationic Acid Phosphatase Isozyme from Rat Liver Mitochondria
- モルモット血清中のo-及びm-Tyrosine含量に及ぼす銅投与の影響
- Hydroxylation of Phenylalanine by Myeloperoxidase-Hydrogen Peroxide System
- Accelerating Effect of Glutathione on Hydroxylation of Phenylalanine by Stimulated Polymorphonuclear Leukocytes
- Tyrosine Formation from Phenylalanine by Ultraviolet Irradiation
- On the Mechanism of Inactivation of Papain by Hydroxylamine
- Studies on the Formation of 3,4-Dihydroxyphenylalanine, m-Tyrosine and o-Tyrosine from L-Phenylalanine by Rat Liver and Adrenal
- Chemical Modification of Essential Histidine Residues in Mn(III)-Acid Phosphatase by Diethylpyrocarbonate in the Presence of F^- Ion(Biological)
- Release of Bases from Deoxyribonucleic Acid by Ascorbic Acid in the Presence of Cu^
- Subcellular Localization and Some Properties of Intermediate-Molecular-Weight Acid Phosphatase from Rat Liver
- In Vivo Studies on the Formation of m-Tyrosine and o-Tyrosine from L-Phenylalanine in Rats
- Acid Dissociation of Tyrosine and Its Related Compounds
- サツマイモに含まれる2種の酸性ホスファターゼの酵素学的, 物理化学的, 免疫学的性質の比較
- Formation of m-Tyrosine and o-Tyrosine from L-Phenylalanine in Various Tissues of Rats
- The Photochemical Decomposition and Hydroxylation of Phenylalanine in the Presence of Riboflavin
- Hydroxylation of Phenylalanine by the Hypoxanthine-Xanthine Oxidase System
- THE FORMATION OF m-TYROSINE AND o-TYROSINE IN RATS
- Chymopapain. I. Oxidation of Tryptophan Residues by N-Bromosuccinimide
- Chymopapain. II. Photooxidation of Histidine Residues
- Quantitative Analysis of Primary Amines by Ion-exchange Chromatography
- Studies on the Active Site of Papain. V. Photooxidation of Histidine Residues
- Studies on the Active Site of Papain. VIII. Photooxidation of Tryptophan Residues
- Studies on the Active Site of Papain. VII. States of Tryptophan Residues
- Studies on the Active Site of Papain. VI. Chemical Modification of Tryptophan Residues by N-Bromosuccinimide
- Studies on Violet-colored Acid Phosphatase : Inactivation of Soybean Enzyme by Cysteine
- Further Studies on the Properties of Violet-colored Acid Phosphatase from Soybean
- Purification and Some Properties of Violet-colored Acid Phosphatase from Spinach Leaves
- Studies on the Hydroxylation of Phenylalanine by 6,7-Dimethyl-5,6,7,8-tetrahydropteridine
- On the Mechanism of Inactivation of Papain by Bisulfite
- The Determination of m-Tyrosine in Human Plasma by High Performance Liquid Chromatography
- Studies on the Hydroxylation of Phenylalanine by the Ascorbic Acid-Hydrogen Peroxide System
- Formation of m-Tyrosine and o-Tyrosine from L-Phenylalanine by Rat Brain Homogenate
- Quantitative Analysis of the Isomers of Hydroxyphenylalanine by High-Performance Liquid Chromatography using a Fluorimetric Detector
- Studies on the Hydroxylation of Phenylalanine by Hydrogen Peroxide in the Presence of Cupric Ions
- Studies on Inactivation of Papain by Ascorbic Acid in the Presence of Cupric Ions
- Nonenzymatic Hydroxylation of Phenylalanine by Ascorbic Acid and Cu^
- Quantitative Analysis of the Isomers of Hydroxyphenylalanine by Ion-exchange Chromatography
- Studies on the Active Site of Papain. II. Inhibition by Cyclic Imide Compounds
- Studies on the Active Site of Papain. I. Inhibition by Barbituric Acid Derivatives with Active Methylene Group and Active Imide Group
- Inactivation of Yeast Alcohol Dehydrogenase by Dehydroascorbic Acid and D-Arabinosone