Hydrolysis of p-nitrophenyl esters catalyzed by N-alkylated polyallylamine.
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Lipoprotein Lipase-catalyzed Hydrolysis of p-Nitrophenyl Butyrate
The mechanism of action of bovine milk lipoprotein lipase (LpL) was studied with a water-soluble substrate of p-nitrophenylbutyrate (PNPB). The calculated maximal velocity ( Vmm) and Michaelis constant (Km) values at 37 "C were 2.0 pmol of p-nitrophenol released/min/ mg of LpL and 0.52 mM, respectively. The addition of phospholipid vesicles enhanced the rate of PNPB hydrolysis by LpL. In the pr...
متن کاملHydrolysis of p-nitrophenyl esters promoted by semifluorinated quaternary ammonium polymer latexes and films.
Semifluorinated polymer latexes were prepared by emulsion polymerization of 2.5-25% of a fluoroalkyl methacrylate, 25% chloromethylstyrene, 1% styrylmethyl(trimethyl)ammonium chloride, and the remainder 2-ethylhexyl methacrylate under surfactant-free conditions. The chloromethylstyrene units were converted to quaternary ammonium ions with trimethylamine. In aqueous dispersions at particle conce...
متن کاملLipoprotein lipase-catalyzed hydrolysis of p-nitrophenyl butyrate. Interfacial activation by phospholipid vesicles.
The mechanism of action of bovine milk lipoprotein lipase (LpL) was studied with a water-soluble substrate of p-nitrophenylbutyrate (PNPB). The calculated maximal velocity ( Vmm) and Michaelis constant (Km) values at 37 "C were 2.0 pmol of p-nitrophenol released/min/ mg of LpL and 0.52 mM, respectively. The addition of phospholipid vesicles enhanced the rate of PNPB hydrolysis by LpL. In the pr...
متن کاملThe trypsin-catalyzed hydrolysis of N alpha-benzyloxycarbonyl-L-lysine p-nitrophenyl ester in dimethylsulfoxide at sub-zero temperatures.
The effect of sub-zero temperatures and aqueous dimethylsulfoxide solutions on the trypsin-catalyzed hydrolysis of N=-benzyloxycarbonyl-L-lysine p-nitrophenyl ester has been investigated. With increasing dimethylsulfoxide concentration at O’, keat decreases in proportion to the decreased water concentration; however, K,,, increases by 2 orders of magnitude. The effect on K,,, can be accounted f...
متن کاملThe reaction of p-nitrophenyl esters with chymotrypsin and insulin.
was discussed. This compound is a member of a group of organophosphorus insecticides which are powerful inhibitors of cholinesterases. They will also inhibit chymotrypsin, and it has been shown that this inhibition is due to combination of the compounds with a single active centre in the enzyme (Jansen, Nutting & Balls, 1949; Hartley & Kilby, 1952).We investigated the reaction ofchymotrypsin wi...
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ژورنال
عنوان ژورنال: KOBUNSHI RONBUNSHU
سال: 1986
ISSN: 0386-2186,1881-5685
DOI: 10.1295/koron.43.59