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• W1999083555 abstract "Phosphatidylethanolamine:dolichol acyltransferase (PEDAT), an enzyme previously partially purified and characterized in rat liver [Sindelar, P., Chojnacki, T., & Valtersson, C. (1992) J. Biol. Chem. 267, 20594-20599], is here purified to homogeneity from a heparin perfusate of rat liver and is shown to be identical to hepatic lipase. However, in contrast to triglyceride hydrolysis by hepatic lipase, the PEDAT activity is strongly dependent on a heat-stable plasma cofactor. This cofactor stimulates the activity up to 15-fold and shifts the pH optimum for the reaction from 8.5 to 7.5. Upon gel filtration on Bio-Gel A-1.5, the factor is heterogeneously distributed, with a major peak at 220 kDa. The dolichol-acylating activity can also be detected in rat adrenals and ovaries, and evidence is presented that the PEDAT assay shows a higher degree of specificity for hepatic lipase than the standard assay with triolein-gum arabic emulsion in 1 M NaCl." @default.
• W1999083555 created "2016-06-24" @default.
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• W1999083555 creator A5068772385 @default.
• W1999083555 date "1993-09-01" @default.
• W1999083555 modified "2023-10-14" @default.
• W1999083555 title "Hepatic lipase acylates dolichol in the presence of a plasma cofactor in vitro" @default.
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• W1999083555 doi "https://doi.org/10.1021/bi00087a032" @default.
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