小原晃 | Kyoto College of Pharmacy

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概要

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著作論文

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
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
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

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