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About This Item
Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-669-1
MDL number:
Nombre del producto
Lipoprotein Lipase from Burkholderia sp., lyophilized powder, ≥50,000 units/mg solid
biological source
Burkholderia spp.
form
lyophilized powder
specific activity
≥50,000 units/mg solid
storage temp.
−20°C
Quality Level
Application
Lipoprotein Lipase from Burkholderia sp. has been used in the subcellular fractionation of mussel Mytilus galloprovincialis to identify the biomolecule attached to cytosolic fraction of okodaic acid. It has also been used to test its effect on serum amyloid A induced granulocyte colony-stimulated factor (G-CSF) expression in response to bacterial lipoprotein.LipoproteinLipase from Burkholderia sp. is suitable for the synthesis ofdiarylmethanols, a precursor for the synthesis of pharmaceutical compounds.
Lipoprotein lipase has been used in a study to assess the role of lipogenic enzymes in colorectal cancer. It has also been used in a study to investigate lipasemic activity of low molecular weight heparin in rats.
Biochem/physiol Actions
Due to its lipolytic activity, lipoprotein lipase was shown to effectively block the spread of hepatitis C virus into healthy cells.
Lipoprotein Lipase (LPL) hydrolysis triacylglycerol moieties in chylomicron and low density lipoproteins. LPL attaches lipoprotein to the vessel wall and facilitates their uptake. Abnormalities in LPL is associated with Alzheimer′s disease, atherosclerosis, obesity and chylomicronaemia.
Lipoprotein lipase belongs to the family of triglyceride lipases. It hydrolyses triglycerides in triglyceride-rich ApoB-containing lipoproteins.
General description
Lipoprotein Lipase (LPL) is a glycerol ester hydrolase. Several bacteria that produce LPL, belongs to the genus Pseudomonas, Serratia and Mucor.
Lipoprotein lipase hydrolyzes triglycerides in plasma lipoproteins causing release of fatty acids for metabolic purposes in muscles and adipose tissue.
Other Notes
One unit will release 1.0 nmole of p-nitrophenol per min at pH 7.2 at 37 °C using p-nitrophenyl butyrate as substrate.
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Maria Notarnicola et al.
Anticancer research, 32(7), 2585-2590 (2012-07-04)
In this review, we summarize recent progress regarding the study of the main enzymes of lipid metabolism involved in colorectal cancer development, namely of a) farnesyltransferase (Ftase), a cytosolic enzyme that catalyzes the first step in the protein farnesylation; b)
Studies on the Lipoprotein Lipases of Microorganisms
Arima K, et al.
Agricultural and Biological Chemistry, 31(8), 924-929 (1967)
Reiner Thomssen et al.
Medical microbiology and immunology, 191(1), 17-24 (2002-07-26)
In most sera of hepatitis C virus (HCV)-infected patients beta-lipoproteins are bound to HCV RNA-carrying material, most often simultaneously with immunoglobulins (IgG, IgM) and sometimes additionally with high-density lipoproteins, forming complexes of low density (1.04-1.06 g/ml). To separate HCV particles
Subcellular distribution of okadaic acid in the digestive gland of Mytilus galloprovincialis: First evidences of lipoprotein binding to okadaic acid
Rossignoli, Araceli E and Blanco, Juan
Toxicon, 55(2-3), 221-226 (2010)
Lipoprotein lipase: from gene to obesity
Wang H and Eckel RH
American Journal of Physiology. Endocrinology and Metabolism, 297(8), E271?E288-E271?E288 (2009)
Contenido relacionado
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