Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

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

Biochem/physiol Actions

Malic dehydrogenase catalyzes the dehydrogenation of L-malate by NAD+.

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

General description

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

Other Notes

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

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)