Studies on the Active Site of Papain. III. Inhibition by Dibasic Acids
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概要
- 論文の詳細を見る
In the previous paper, it was reported that the cyanide-activated papain is apparently inhibited by active methylene group and active imide group in barbituric acid. The active methylene group in barbituric acid is derived from malonic acid. Morgan and Friedmann have been shown that maleic acid and SH-compounds interact with the formation of stable addition compounds. They have applied this reaction to the study of some SH-enzyme reaction. The present research has been planed to clarify relation between activity of papain and influence of the dibasic acids.
- 社団法人日本薬学会の論文
- 1970-09-25
著者
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石光 進
Kyoto Phramaceutical Univeristy
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玉井 敏夫
Kyoto College Of Pharmacy
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金沢 治男
Kyoto College of Pharmacy
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清水 康紘
Kyoto College of Pharmacy
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田中 茂
Kyoto College of Pharmacy
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小原 晃
Kyoto College of Pharmacy
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吉岡 政七
Kyoto College of Pharmacy
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田中 茂
Central Research Laboratories Sankyo Co. Ltd.
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金沢 治男
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
- Reaction of Ethyl Acetoacetate with Isoquinolinium and Pyridinium Ylides
- 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
- 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
- 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
- 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
- Synthesis of Methylpyridine Derivatives. XXVII. Synthesis of 1,3-Disubstituted-4-oxo-quinolizine and 2,4-Disubstituted-1-oxo-benzo [c] quinolizine Derivatives
- 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
- Formation of Triazole and Isoxazole Derivatives from β-Substituted Pyridinium Salts
- Formation of Pyrazole Derivatives from β-Substituted Pyridinium Salts
- 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