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Sigma-Aldrich

Lipase Substrate

for the titrimetric determination of enzyme activity

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.32

grade

for the titrimetric determination of enzyme activity

Quality Level

form

liquid

technique(s)

titration: suitable

refractive index

n20/D 1.36

density

1.05 g/mL at 20 °C

storage temp.

2-8°C

Physical form

aqueous solution with 4.5 mM triolein; 1 M NaCl; 13% (w/v) Triton X-100

Other Notes

Assay of microbial lipases with emulsified trioleoyl glycerol; the fatty acids released are titrated with a pH stat

Legal Information

Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


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A new assay of microbial lipases with emulsified trioleoyl glycerol.
N Peled et al.
Analytical biochemistry, 112(2), 219-222 (1981-04-01)
H Schmidinger et al.
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
Hannes Schmidinger et al.
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
G Hofer et al.
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
H Scholze et al.
Analytical biochemistry, 276(1), 72-80 (1999-12-10)
We report on the determination of active enzyme components in pure and crude lipases, using fluorescent inhibitors for covalent modification and visualization of the enzymatically active proteins. Lipase-specific compounds are triacylglycerol analogs, namely 1,2(2, 3)-di-O-alkylglyceroalkylphosphonic acid-p-nitrophenyl esters, containing a fluorescent

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