62335

Lipoprotein Lipase from Pseudomonas sp.

lyophilized, powder, ≥1200 U/mg

• CAS Number: 9004-02-8
• Enzyme Commission number: 3.1.1.34 (BRENDA, IUBMB)
• EC Number: 232-669-1
• MDL number: MFCD00131523
• UNSPSC Code: 12352204
• NACRES: NA.54

Properties

• biological source: bacterial (Pseudomonas spp.)
• Quality Level: 100
• form: powder
• quality: lyophilized
• specific activity: ≥1200 U/mg
• storage temp.: −20°C

Description

General description

Lipoprotein Lipase (LPL) is majorly secreted by myocytes and adipocytes in humans and is crucial for triglyceride homeostatis.[1] Mutations in the catalytic domain of LPL impairs its interaction with glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPIHBP1).[2] The N-terminal catalytic domain is essential for lipolysis. The C-terminal is crucial for binding lipoproteins. Altered LPL levels may play role in the pathogenesis of atherosclerosis, coronary heart disease and chronic lymphocytic leukemia.[3]

Application

Lipoprotein Lipase from Pseudomonas sp. has been used in the enzymatic erosion studies in gamma irradiated poly(trimethylene carbonate) (PTMC) films.[4]

Biochem/physiol Actions

Malic dehydrogenase catalyzes the dehydrogenation of L-malate by NAD+.[5][6]

Lipoprotein lipase belongs to the family of triglyceride lipases.[7] It hydrolyses triglycerides in triglyceride-rich ApoB-containing lipoproteins.[8]

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol oleic acid per minute at pH 8.0 and 40°C (triolein, Cat. No. 62314 as substrate)

Other Notes

Preparation of aldol acceptors (R)- and (S)-3-azido-2-hydroxypropanal via lipase-catalyzed resolution of the racemic acetal precursor[9]; Effect of enzyme form on its properties in toluene[10]

Safety Information

• 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