Purification and Kinetic Properties of Guinea Pig Liver β-Mannosidase

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概要

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• β-Mannosidase was purified to electrophoretic homogeneity from the 20000g supernatant of guinea pig liver homogenate. A highly purified enzyme preparation was also obtained from the acetone powder. This enzyme had a pH optimum of 4.0 and molecular weights of ca. 120000 as determined by gel filtration and 110000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It was free from other glycosidase activities, as far as was tested. The enzymatic hydrolysis of o- and p-nitrophenyl β-mannosides exhibited an unusual relationship of rate to substrate concentration, indicative of the involvement of two molecules of substrate in the reaction. The rate of hydrolysis was enhanced markedly by several p-nitrophenyl compounds including p-nitrophenyl glycosides, and also by Triton X-100 and chlorinated pesticides such as aldrin.

• 社団法人日本薬学会の論文
• 1985-01-25

著者

• 京坂 重久

  School of Pharmaceutical Science, Toho University

• 村田 早苗

  School of Pharmaceutical Science, Toho University

• 田中 光也

  School of Pharmaceutical Science, Toho University

• 田中 光也

  School Of Pharmaceutical Sciences Toho University

• 中村 史子

  School of Pharmaceutical Science, Toho University

• 中村 史子

  School Of Pharmaceutical Science Toho University:(present Address)nippon Chemicals Co. Ltd.

• 京坂 重久

  School Of Pharmaceutical Sciences Toho University

• 村田 早苗

  School Of Pharmaceutical Science Toho University

関連論文

• Isolation and Identification of Self-Transfer Products Formed by Guinea Pig Liver β-Mannosidase(Organic,Chemical)
• Kinetic Study on the Binding of 1,1,1-Trichloro-2,2-bis(4-chlorophenyl)ethane to Rhizopus delemar C-Lipase : Rate Constants and the Effect of Slow Addition of the Ligand on Complex Formation
• Tryptophan Residues Involved in the Binding of Chlorinated Pesticides by Rhizopus delemar C-Lipase : Isolation of Tryptophan-Containing Peptides
• Modification of Tryptophan Residues on Rhizopus delemar C-Lipase Binding Chlorinated Pesticide by 2-Hydroxy-5-nitrobenzylation
• Interaction of Rhizopus delemar Lipase with 1,1,1-Trichloro-2,2-bis(4-chlorophenyl)ethane and Structurally Related Pesticides : Importance of 1 : 1 Pesticide-Lipase Complexes
• Selective Measurement of Hepatic Triglyceride Lipase and Lipoprotein Lipase in Rat Postheparin Plasma with Pentachlorophenol and Dichlorodiphenyltrichloroethane(Biological)
• Purification and Kinetic Properties of Guinea Pig Liver β-Mannosidase
• Adsorption of Some β-Glycosidases on N-(g-Aminohexanoyl)-β-D-glycosylamine-agarose
• Purification and Kinetic Studies of β-Acetylhexosaminidase A from Porcine Kidney
• Bovine Liver β-Acetylhexosaminidase Molecular Weight and Subunit Composition
• Bovine Liver β-Acetylhexosaminidase. Purification by Hydrophobic Affinity Chromatography and Heterogeneity
• Purification and Some Properties of Bovine Liver β-Acetylhexosaminidase
• Effect of Substituents on the Hydrolysis of Substituted Phenyl β-Acetylglucosaminides by Bovine Liver β-Acetylglucosaminidase
• The Rates of Hydrolysis of Some Substituted Phenyl 2-Acetamido-2-deoxy-α-and-β-D-glucopyranosides
• Syntheses of N-Aminoacyl-D-glucosamine Derivatives and Periodate Oxidation Thereof
• Rates of Acidic and Alkaline Hydrolysis of Substituted Phenyl α-and β-D-Mannopyranosides

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