Homology of lipoprotein lipase to pancreatic lipase.
نویسندگان
چکیده
منابع مشابه
Chimeras of Hepatic Lipase and Lipoprotein Lipase
Chimeric molecules between human lipoprotein lipase (LPL) and rat hepatic lipase (HL) were used to identify structural elements responsible for functional differences. Based on the close sequence homology with pancreatic lipase, both LPL and HL are believed to have a two-domain structure composed of an aminoterminal (NHz-terminal) domain containing the catalytic Ser-His-Asp triad and a smaller ...
متن کاملStudies of fat lipolysis by post-heparin human plasma lipoprotein lipase and by human pancreatic lipase.
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Activation of Lipoprotein Lipase
Lipoprotein lipase (LPL) from rat heart acetone powders has been reported to depend on the presence of NH4 + , calcium, or other divalent cations for optimal activity. In addition, the enzyme will not hydrolyze an artificial triglyceride emulsion unless it is converted to an active substrate by the addition of very low density lipoproteins, high density lipoproteins (HDL), or certain peptides c...
متن کاملLipoprotein lipase and atherosclerosis.
Lipoprotein lipase (LPL) is a rate-limiting enzyme that hydrolyzes circulating triglyceride-rich lipoprotein such as very low density lipoproteins and chylomicrons. A decrease in LPL activity is associated with an increase in plasma triglycerides (TG) and decrease in high density lipoprotein (HDL) cholesterol. The increase in plasma TG and decrease in HDL cholesterol are risk factors of coronar...
متن کاملLipoprotein lipase and obesity
Obesity is one of the fast-growing major diseases in developed and developing countries. As has been persuasively argued, long-term imbalance between intake and expenditure of fat is a central factor in the etiology of obesity. Obesity aggravates insulin resistance and promotes cardiovascular diseases and atherosclerosis. We hypothesized that elevating lipoprotein lipase (LPL) activity in skele...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1986
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.83.12.4185