Studies on the Mechanism of Lipase Reaction. III. Adsorption of Chromobacterium Lipase on Hydrophobic Glass Beads
スポンサーリンク
概要
- 論文の詳細を見る
The lipase from Chromobacterium was adsorbed on glass beads which was coated with olive oil, liquid paraffin or silicone oil. These adsorption was treated in the Lineweaver-Burk's plot and characters of the adsorption were similar each other regardless of their chemical structure of hydrophobic materials. On the other hand, esterase from porcine liver was not adsorbed on hydrophobic glass beads. The interaction between the lipase and hydrophobic surface conformed to the Langmuir's adsorption isotherm with a dissociation constant K=1.4×10^<-7>M. At saturation of the surface with the lipase each protein molecule occupies an average area of 4500 A^2 per molecule. The lipase adsorbed on hydrophobic surface did not inactivated but activated about 3-fold. It was elucidated that the hydrophobic bond play a major role in the adsorption of the lipase on substrate or hydrophobic surface.
- 公益社団法人日本薬学会の論文
- 1976-01-25
著者
関連論文
- Antitumor Polysaccharide Fraction from Sargassum thunbergii
- Chemical Structure of Antitumor Polysaccharide, Coriolan, produced by Coriolus versicolor
- Chemical Modification of Tryptophan and Histidine Residues in Lipoprotein Lipase from Pseudomonas fluorenscens
- Studies on Inactivation of the Semi-alkaline Proteinase from Aspergillus melleus
- Purification of Microbial Lipases by Glass Beads coated with Hydrophobic Materials
- Studies on the Lipase of Chromobacterium viscosum. V. Physical and Chemical Properties of the Lipases
- Studies on the Mechanism of Lipase Reaction. IV. Action of the Lipase from Chromobacterium on Monomeric p-Nitrophenyl Acetate
- Studies on the Mechanism of Lipase Reaction. III. Adsorption of Chromobacterium Lipase on Hydrophobic Glass Beads
- Studies on Dextranase. VIII. Some Enzymatic Properties of Immobilized Dextranase from Brevibacterium fuscum var. dextranlyticum
- Studies on Dextranase. VII. The Kinetic Parameters of Brevibacterium fuscum Dextranase and Molecular Properties of the Digestion Products
- Application of Lipoprotein Lipase for the Assay of Serum Triglyceride
- Studies on Dextranase. VI. Some Physicochemical Properties and Amino Acid Compositions of Dextranases from Brevibacterium fuscum var. dextranlyticum and Penicillium funiculosum IAM 7013
- Studies on the Lipase of Chromobacterium viscosum. IV. Substrate Specificity of a Low Molecular Weight Lipase
- Studies on the Mechanism of Lipase Reaction. I. Inhibition of Lipase Activity by Emulsion of Organic Solvents
- Effects of Temperature and State of Substrate on the Rate of Hydrolysis of Glycerides by Lipase
- Studies on Dextranase. IV. Immobilization of Dextranase from Penicillium funiculosum IAM 7013
- Studies on Dextranase. III. Action Patterns of Dextranase from Penicillium funiculosum on Substrate and Inhibition on Hydrolysis Reaction by Substrate Analogues
- Studies on Bile-sensitive Lipase. X. Preparation and Properties of Carrier-bound Mucor Lipase
- Sterol Ester Hydrolytic Activity of Lipoprotein Lipase from Pseudomonas fluorescence
- Pharmaceutical Studies on β-Galactosidases from Macrophomina phaseoli and Sclerotium tuliparum
- Stability of Retinol Analogs. VIII. Pyrolysis and Photolysis of Retinoic Acid in Aqueous Ethanolic Solution
- Purification of Alkaline Phosphatase from Human Liver