Studies on the Active Site of Papain. V. Photooxidation of Histidine Residues
スポンサーリンク
概要
- 論文の詳細を見る
1) The present research has been planed to demonstrate the importance of histidine residues on enzyme activity of papain by means of photooxidation. 2) Papain was rapidly inactivated by methylene blue-sensitized photooxidation. 3) The rate of photo-sensitized inactivation was pH dependent, and about one histidine residue per molecule of papain was lost when complete inactivation took place. 4) Mercuripapain was not inactivated by methylene blue-sensitized photooxidation, and the histidine residue was not affected in the illuminated mercuripapain. 5) These results indicate that the modification of a histidine residue by photooxidation cause loss of the enzyme activity for hydrolysis of benzoyl-L-arginine amide. 6) The state of the histidine residue in the active site of papain is discussed to explain the results of the photooxidation studies described here.
- 公益社団法人日本薬学会の論文
- 1975-05-25
著者
-
小原 晃
Kyoto College of Pharmacy
-
藤本 貞毅
Kyoto Pharmaceutical University
-
藤本 貞毅
Laboratory Of Biochemistry Kyoto Pharmaceutical University
-
金澤 治男
Kyoto Pharmaceutical University
-
Kanazawa H
Dept. Biotechnology Faculty Of Engineering Sciences
-
金澤 治男
Kyoritsu College Of Pharmacy
-
中川 力
Kyoto College of Pharmacy
-
中川 力
Giba-geigy (japan) Limited
関連論文
- Studies on the Active Site of Papain. III. Inhibition by Dibasic Acids
- pH-Dependent Growth Retardation of Escherichia coli Caused by Overproduction of Na^+/H^+ Antiporter
- Identification and Characterization of Functional Residues in a Na^+/H^+ Antiporter (NhaA) from Escherichia coli by Random Mutagenesis^1
- 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
- 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
- Determination of α-Tocopherol and α-Tocopherylquinone in Rat Tissues and Plasma by High-Performance Liquid Chromatography with Electrochemical Detection
- Chymopapain. I. Oxidation of Tryptophan Residues by N-Bromosuccinimide
- Chymopapain. II. Photooxidation of Histidine Residues
- Quantitative Analysis of Primary Amines by Ion-exchange Chromatography
- Species Absorbing in the 500-nm Region in the Reactions of Pyridoxamine with Pyrroloquinoline Quinone and Phenathrolinequinones
- HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY OF SAPONINS OF CRUDE DRUGS ON CHEMICALLY MODIFIED POROUS GLASS
- 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
- Studies on the Active Site of Papain. IV. Influence of Dehydroascorbic Acid and Ascorbic Acid
- Inactivation of Yeast Alcohol Dehydrogenase by Dehydroascorbic Acid and D-Arabinosone