62314
Lipase Substrate
for the titrimetric determination of enzyme activity
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.32
Recommended Products
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 Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), 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)
Hannes Schmidinger et al.
Chembiochem : a European journal of chemical biology, 7(3), 527-534 (2006-02-14)
Protein and small-molecule microarrays are useful tools for high-throughput analysis of DNA-protein, protein-protein, and protein-small molecule interactions. Here we report on novel microarrays for activity screening of lipases and esterases based on phosphonic acid ester inhibitors. These compounds are activity
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
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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