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  • Title: Identification of the bile acid binding proteins in human serum by photoaffinity labeling.
    Author: Kramer W.
    Journal: Biochim Biophys Acta; 1995 Aug 03; 1257(3):230-8. PubMed ID: 7647099.
    Abstract:
    The binding of conjugated and unconjugated bile acids to human serum lipoproteins was investigated by density gradient centrifugation and photoaffinity labeling studies. The binding of bile acids to high-density lipoprotein increased by substitution of the 3 alpha-hydroxy group in cholate and taurocholate by a photolabile 3-azido or 3-azi-function. The affinity of bile acid derivatives to HDL showed the following ranking: 3 beta-azido-7 alpha,12 alpha-dihydroxy-,3,3-azo-7 alpha,12 alpha-dihydroxy- > 3 alpha,7 alpha,12 alpha-trihydroxy-,11 xi-azido-3 alpha,7 alpha,12 xi-trihydroxy- > 11 xi-azido-12-oxo-3 alpha,7 alpha-dihydroxy- > 7,7-azo-3 alpha,12 alpha-dihydroxy-,3 alpha,7 alpha-dihydroxy-,3 alpha,12 alpha-dihydroxy- > 3 alpha-hydroxy-cholan-24-oic acid. Based on the actual serum concentrations of albumin and HDL, a preference of hydrophilic bile acids to HDL is evident, the 3-azido- and 3-azi-derivatives showing a 5-23-fold higher binding to HDL compared to soluble serum proteins. For the identification of the bile acid binding proteins in human blood, photoaffinity labeling with a variety of photolabile conjugated and unconjugated bile acid derivatives was performed with subsequent analysis of radiolabeled serum proteins by one- and two-dimensional gel electrophoresis. In addition to albumin and the apolipoproteins A-I and A-II of high-density lipoproteins (Kramer et al. (1979) Eur. J. Biochem. 102, 1-9), three further proteins in the lipoprotein free serum fraction of M(r) 41,000, 50,000 and 83,000 were specifically labeled. By two-dimensional electrophoresis and by immunoprecipitation these proteins were identified as alpha 1-acid glycoprotein (M(r) 41,000), alpha 1-antitrypsin (M(r) 50,000) and transferrin (M(r) 83,000). No binding of bile acids to haptoglobin, alpha 2-HS-glycoprotein, hemopexin or alpha 1-fetoprotein occurred. In conclusion, these studies show that bile acid derivatives bind to several serum proteins in addition to albumin and furthermore that the substituent in position 3 of the steroid nucleus greatly influences the affinity of bile acids to high density lipoproteins.
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