Detection and characterization of anionic polypeptidic fraction binding sites in rat liver plasma membranes and cultured hepatocytes
Identifieur interne : 000180 ( France/Analysis ); précédent : 000179; suivant : 000181Detection and characterization of anionic polypeptidic fraction binding sites in rat liver plasma membranes and cultured hepatocytes
Auteurs : M. Martigne [France] ; B. Melin [France] ; F. Mahlberg ; N. Domingo [France] ; F. Chanussot [France] ; H. Lafont [France] ; J. C. Hauton [France]Source :
- BBA - Biomembranes [ 0005-2736 ] ; 1988.
English descriptors
- KwdEn :
Abstract
The binding of human 125I-labeled ‘anionic polypeptidic fraction’ (APF) to purified rat liver plasma membranes was studied. The dissociation constant for this binding was 3.0 μg protein/mg membrane protein. Binding was competitively inhibited by unlabeled human APF, but not by human LDL (low density lipoproteins). When unlabeled HDL3 was added, binding of labeled APF was competitively reduced to a level between that of unlabeled APF and unlabeled LDL. Experiments with cultured rat hepatocytes confirmed those obtained with liver membranes and suggested the presence in rat liver of saturable APF-binding sites which seem to be specific for APF. The physiologic significance of these APF binding sites is discussed in relation to the fate of cholesterol in the liver.
Url:
DOI: 10.1016/0005-2736(89)90254-X
Affiliations:
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ISTEX:E1513F8B6ECC1A4E5099BE6E8D6EB4D77FCAFF1CLe document en format XML
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