Rat liver contains a limited number of binding sites for hepatic lipase
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چکیده
منابع مشابه
Rat liver contains a limited number of binding sites for hepatic lipase.
The binding of hepatic lipase to rat liver was studied in an ex vivo perfusion model. The livers were perfused with media containing partially purified rat hepatic lipase or bovine milk lipoprotein lipase. The activity of the enzymes was determined in the perfusion media before and after passage through the liver. During perfusion with a hepatic-lipase-containing medium the lipase activity in t...
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Hepatic lipase (HL) plays a key role in the metabolism of several lipoproteins. Metabolically active HL is bound in liver parenchymal cells to specific binding sites. We studied the nature of the HL binding in rat liver. Rat livers were perfused with heparin, which lead to a loss of 80% of the HL binding capacity of the liver. The heparin-containing perfusates possessed HL binding capacity, det...
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Rat hepatic triglyceride lipase was expressed as a bacterial fusion protein and as a secreted protein in eukaryotic cells. The bacterial fusion construct coded for seven amino acids at the N-terminus which are not present in the hepatic lipase cDNA, but otherwise consisted of only the complete mature lipase sequence. Fusion protein was isolated as an insoluble product which did not have lipase ...
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It has been reported that rat liver cystathionase (EC 4.4.1 .l) is inhibited by butanedione and suggested that the a-carboxyl groups of the substrates (L-homoserine and L-cysteine, respectively) are bound to the protein through arginine residues [I]. To support the concept that specific residues are critical or even essential to enzyme activities, we carried out experiments using phenylglyoxal,...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1994
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3020717