62314
Lipase-Substrat
for the titrimetric determination of enzyme activity
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About This Item
Empfohlene Produkte
Qualität
for the titrimetric determination of enzyme activity
Form
liquid
Methode(n)
titration: suitable
Brechungsindex
n20/D 1.36
Dichte
1.05 g/mL at 20 °C
Lagertemp.
2-8°C
Physikalische Form
wässrige Lösung mit 4.5 mM Triolein; 1 M NaCl; 13% (G/V) Triton X-100
Sonstige Hinweise
Assay of microbial lipases with emulsified trioleoyl glycerol; the fatty acids released are titrated with a pH stat
Rechtliche Hinweise
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves
Analysenzertifikate (COA)
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A new assay of microbial lipases with emulsified trioleoyl glycerol.
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Amino acids, 30(4), 333-350 (2006-06-15)
In the postgenomic era new technologies are emerging for global analysis of protein function. The introduction of active site-directed chemical probes for enzymatic activity profiling in complex mixtures, known as activity-based proteomics has greatly accelerated functional annotation of proteins. Here
Free radical research, 23(4), 317-327 (1995-10-01)
We report on a new method for the determination of lipid oxidation in lipoproteins and plasma. The biological lipid system is preloaded with a fluorescent analog of phosphatidylcholine containing diphenylhexatriene (DPH) propionic acid covalently linked to the sn-2 position. When
Chembiochem : a European journal of chemical biology, 6(10), 1776-1781 (2005-08-12)
Lipases and esterases are responsible for carboxylester hydrolysis inside and outside cells and are useful biocatalysts for (stereo)selective modification of synthetic substrates. Here we describe novel fluorescent suicide inhibitors that differ in structure and polarity for screening and discrimination of
Methods in molecular biology (Clifton, N.J.), 579, 497-511 (2009-09-19)
Lipases are responsible for the hydrolysis of acylglycerols and cholesteryl esters in animals, plants, and microorganisms. In this chapter we describe a tool for the concomitant analysis of lipases in complex proteomes. For this purpose, the target enzymes are selectively
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