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L9656

Sigma-Aldrich

Lipoprotein Lipase from Burkholderia sp.

lyophilized powder, ≥50,000 units/mg solid

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Synonym(s):
Diacylglycerol acylhydrolase, Diacylglycerol lipase, Lipoprotein Lipase from Pseudomonas sp.
CAS Number:
9004-02-8
Enzyme Commission number:
3.1.1.34 (BRENDA, IUBMB)
EC Number:
232-669-1
MDL number:
MFCD00131523
NACRES:
NA.54

biological source

Burkholderia spp.

Quality Level

200

form

lyophilized powder

specific activity

≥50,000 units/mg solid

storage temp.

−20°C

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.

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.
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.

Unit Definition

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Studies on the Lipoprotein Lipases of Microorganisms
Arima K, et al.
Agricultural and Biological Chemistry, 31(8), 924-929 (1967)
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)
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)
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
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