Studies on the Active Site of Papain. VI. Chemical Modification of Tryptophan Residues by N-Bromosuccinimide
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 tryptophan residues on enzyme activity of papain by means of NBS oxidation. 2) About 2 tryptophan residues were oxidized and the first oxidizable tryptophan was important for enzyme activity. 3) The relationship between tryptophan oxidation and enzyme activity for acetylpapain and mercuripapain are quite similar to that for papain. 4) About 1 tryptophan and 3 tyrosine residues in papain were modified by NBS oxidation. However, only 1 tryptophan residue and no tyrosine residue in acetylpapain were oxidized at complete inactivation. 5) The acetylation of tyrosine in papain prevented the tyrosine from oxidizing by NBS. 6) SH group and histidine residues in papain were not affected by NBS oxidation. 7) These results indicate that the modification of a tryptophan residue by NBS oxidation causes loss of the enzyme activity.
- 公益社団法人日本薬学会の論文
- 1975-08-25
著者
-
小原 晃
Kyoto College of Pharmacy
-
金澤 治男
Kyoto Pharmaceutical University
-
坂根 万純
Kyoto College of Pharmacy
-
金澤 治男
Kyoritsu College Of Pharmacy
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
- On the Mechanism of Inactivation of Active Papain by Ascorbic Acid in the Presence of Cupric Ions
- 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
- Hydroxylation of Phenylalanine by Myeloperoxidase-Hydrogen Peroxide System
- 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
- 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
- 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