| Literature DB >> 3029530 |
Abstract
Bile acids solubilize proteins from liver plasma membrane both in vivo and in vitro. The ability to solubilize the proteins is dependent on the species of bile acid. In this paper, the effect of phospholipid on the solubilization of a membrane-bound enzyme by bile acids was investigated in vitro. Taurocholate (TC) and tauroursodeoxycholate (TUDC) solubilized the enzyme, 5'-nucleotidase, from the liver plasma membrane of the rat in a concentration-dependent manner, although there was a great difference in their effect; at 40 mM, TC solubilized 55.4% of the original 5'-nucleotidase activity of the membrane, but TUDC only 5.7%. While lecithin alone had no solubilizing effect, its addition to the bile acids provoked a 10-fold increase in the solubilizing effect of TUDC, but virtually no change for TC, essentially equalizing the solubilizing effect of the two. Both TC-rich and TUDC-rich bile were obtained from rats infused with the respective bile acids via the jugular vein after their endogenous bile acid pool had been depleted. The solubilization effect of these biles was quite similar to the bile acid-lecithin mixtures. These findings demonstrate that lecithin enhances the ability of the bile acids to solubilize the membrane protein and eliminates the difference in the two bile acid species in their solubilizing ability.Entities:
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Year: 1987 PMID: 3029530 DOI: 10.1007/BF02534873
Source DB: PubMed Journal: Lipids ISSN: 0024-4201 Impact factor: 1.880