62314
Lipase Substrate
for the titrimetric determination of enzyme activity
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About This Item
Código UNSPSC:
12352204
NACRES:
NA.32
Produtos recomendados
grau
for the titrimetric determination of enzyme activity
Nível de qualidade
forma
liquid
técnica(s)
titration: suitable
índice de refração
n20/D 1.36
densidade
1.05 g/mL at 20 °C
temperatura de armazenamento
2-8°C
forma física
aqueous solution with 4.5 mM triolein; 1 M NaCl; 13% (w/v) Triton™ X-100
Outras notas
Assay of microbial lipases with emulsified trioleoyl glycerol; the fatty acids released are titrated with a pH stat
Informações legais
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
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, 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 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
Maximilian Schicher et al.
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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