脂蛋白脂酶来源于假单胞菌属，Lipoprotein Lipase from Pseudomonas sp.；lyophilized, powder, ≥1200 U/mg

General description

Lipoprotein Lipase (LPL) is majorly secreted by myocytes and adipocytes in humans and is crucial for triglyceride homeostatis.^[5] Mutations in the catalytic domain of LPL impairs its interaction with glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPIHBP1).^[6] 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.^[7]

Application

Lipoprotein Lipase from Pseudomonas sp. has been used in the enzymatic erosion studies in gamma irradiated poly(trimethylene carbonate) (PTMC) films.^[8]

Biochem/physiol Actions

Malic dehydrogenase catalyzes the dehydrogenation of L-malate by NAD+.^[1][2]

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

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^[3]; Effect of enzyme form on its properties in toluene^[4]

性质

安全信息