Rapid three-step purification of a hepatic neutral cholesteryl ester hydrolase which is not the pancreatic enzyme.
Lipids
; 26(10): 793-8, 1991 Oct.
Article
en En
| MEDLINE
| ID: mdl-1795600
A rat liver cytosolic cholesteryl ester hydrolase (CEH) was purified 12,600-fold by ammonium sulfate precipitation, cation exchange chromatography and gel permeation high-performance liquid chromatography, with an overall yield of 20%. Its properties are compared to those of pancreatic CEH, with which it has sometimes been identified. Liver CEH exhibited a single silver stained band following SDS-polyacrylamide gel electrophoresis (Mr = 66 kDa), was activated by 0.5-10 mM taurocholate but was strongly inhibited by higher levels of taurocholate, which activate pancreatic CEH. Whereas bile salts are known to induce formation of a hexamer of pancreatic CEH, in the current study, 0.5 mM taurocholate dissociated a multimeric form of liver CEH to monomer. Liver CEH did not coelute with pancreatic CEH from cation exchange and chromatofocusing columns, exhibited no immunoreactivity with anti-rat pancreatic CEH IgG in Western blots, was not inhibited by anti-rat pancreatic CEH IgG and had a different amino acid composition from pancreatic CEH. In contrast to liver CEH, which is known to be activated by protein kinases A and C, pancreatic CEH was unaffected by cofactors for protein kinase A and was inhibited by cofactors for protein kinase C.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Esterol Esterasa
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Hígado
Límite:
Animals
Idioma:
En
Revista:
Lipids
Año:
1991
Tipo del documento:
Article
Pais de publicación:
Estados Unidos