Studies on Violet-colored Acid Phosphatase : Inactivation of Soybean Enzyme by Cysteine

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概要

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• The properties of soybean (Glycine max) acid phosphatase, violet-colored and manganese-containing, were further studied. The enzyme was significantly inactivated by the treatment with cysteine in alkaline solution. The enzyme was more inactivated under an aerobic condition than under an anaerobic condition. The inactivation was accompanied by the reduction of the absorbance of the enzyme at 540nm. The mechanisms of the inactivation were also discussed.

• 1979-02-25

著者

• 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

• 中川 力

  Kyoto College of Pharmacy

• 中川 力

  Giba-geigy (japan) Limited

関連論文

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• 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
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• 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
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• 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
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• Inactivation of Yeast Alcohol Dehydrogenase by Dehydroascorbic Acid and D-Arabinosone

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