Irreversible inhibition of pancreatic lipase by bis-p -nitrophenyl methylphosphonate
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چکیده
منابع مشابه
Irreversible inhibition of biotin transport in yeast by biotinyl-p-nitrophenyl ester.
Biotinyl-p-nitrophenyl ester (BNP), an active-ester derivative of biotin, irreversibly inactivates biotin transport in the yeast Saccharomyces cerevisiae. Transport inactivation is progressive with time and occurs at concentrations of the ester as low as 10(-7) M. In the presence of sodium azide, a reagent known to block biotin accumulation in yeast, the derivative is still effective. The speci...
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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...
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The alkyl fluorophosphonates were first shown in 1940 (Adrian, Feldberg & Kilby, 1947) to be very powerful inhibitors of cholinesterase, and for a time they were thought to be quite specific for this enzyme. Later, other esterases, such as human milk lipase and liver esterase (Webb, 1948) and citrus acetylesterase (Jansen, Nutting & Balls, 1947) were also shown to be inhibited, although not to ...
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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...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1985
ISSN: 0014-5793
DOI: 10.1016/0014-5793(85)80605-0