We are analyzing https://link.springer.com/article/10.1007/bf02533857.

Title:
Bile acids in tissues: Binding of lithocholic acid to protein | Lipids
Description:
Human liver contains two forms of lithocholic acid. One form is readily extractable by 95% ethanol/0.1% ammonia (soluble lithocholate, SL), while the other remains firmly bound to the residue (tissue-bound lithocholate, TBL). TBL could be hydrolytically released using clostridial cholanoylamino acid hydrolase, suggesting a peptide link between lithocholate and protein. With bovine serum albumin (BSA), lithocholic acid showed spontaneous amino group-modifying activity. When small molecular weight lysine (α-t-BOC-1-lysyl-β-naphthylamide) and arginine peptides (α-CBZ-di-arginyl-β-naphthylamide) were used in place of BSA, lithocholate bound specifically to the lysine peptide. The unusual affinity for lysine suggested that this amino acid might be involved as a residue in TBL. Synthesis of lithocholyl lysines and comparison with products of acid hydrolysis of TBL established ε-lithocholyl lysine as the predominant form in which lithocholic acid is found in tissue bound form.
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Keywords {🔍}

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Topics {✒️}

α-t-boc-1-lysyl-β-naphthylamide α-cbz-di-arginyl-β-naphthylamide 12α-dihydroxy-5β-cholan-24-oyl glycine 12α-trihydroxy-5β-cholan-24-oyl glycine 3β-hydroxy-5β-cholan-24-oic acid 12α-hydroxy-5β-cholan-24-oic acid 12α-dihydroxy-5β-cholan-24-oic acid 12α-trihydroxy-5β-cholan-24-oic acid 7α-dihydroxy-5β-cholan-24-oyl glycine 3α-hydroxy-5β-cholan-24-oyl glycine 7α-dihydroxy-5β-cholan-24-oic acid 3α-hydroxy-5β-cholan-24-oic acid 3-keto-5β-cholan-24-oic acid 12-triketo-5β-cholan-24-oic acid 5β-cholan-24-oic acid month download article/chapter 12α-hydroxycholanic acid bile acids presented bile acids referred chenodeoxycholic acid cholic acid glycocholic acid full article pdf �bile salt metabolism privacy choices/manage cookies related subjects amino acid bile acids lithocholic acid european economic area remains firmly bound bovine serum albumin phase systems revealed gomprecht hepatitis fund conditions privacy policy lysine peptide tissue-bound lithocholate lithocholate bound specifically accepting optional cookies tissue bound form protein binding affinities article lipids check access instant access article nair main content log journal finder publish peptide link article log acid hydrolysis

Schema {🗺️}

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         description:Human liver contains two forms of lithocholic acid. One form is readily extractable by 95% ethanol/0.1% ammonia (soluble lithocholate, SL), while the other remains firmly bound to the residue (tissue-bound lithocholate, TBL). TBL could be hydrolytically released using clostridial cholanoylamino acid hydrolase, suggesting a peptide link between lithocholate and protein. With bovine serum albumin (BSA), lithocholic acid showed spontaneous amino group-modifying activity. When small molecular weight lysine (α-t-BOC-1-lysyl-β-naphthylamide) and arginine peptides (α-CBZ-di-arginyl-β-naphthylamide) were used in place of BSA, lithocholate bound specifically to the lysine peptide. The unusual affinity for lysine suggested that this amino acid might be involved as a residue in TBL. Synthesis of lithocholyl lysines and comparison with products of acid hydrolysis of TBL established ε-lithocholyl lysine as the predominant form in which lithocholic acid is found in tissue bound form.
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            Cholic Acid
            Chenodeoxycholic Acid
            Lithocholic Acid
            Glycocholic Acid
            Lipidology
            Neurochemistry
            Medical Biochemistry
            Nutrition
            Medicinal Chemistry
            Microbial Genetics and Genomics
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      headline:Bile acids in tissues: Binding of lithocholic acid to protein
      description:Human liver contains two forms of lithocholic acid. One form is readily extractable by 95% ethanol/0.1% ammonia (soluble lithocholate, SL), while the other remains firmly bound to the residue (tissue-bound lithocholate, TBL). TBL could be hydrolytically released using clostridial cholanoylamino acid hydrolase, suggesting a peptide link between lithocholate and protein. With bovine serum albumin (BSA), lithocholic acid showed spontaneous amino group-modifying activity. When small molecular weight lysine (α-t-BOC-1-lysyl-β-naphthylamide) and arginine peptides (α-CBZ-di-arginyl-β-naphthylamide) were used in place of BSA, lithocholate bound specifically to the lysine peptide. The unusual affinity for lysine suggested that this amino acid might be involved as a residue in TBL. Synthesis of lithocholyl lysines and comparison with products of acid hydrolysis of TBL established ε-lithocholyl lysine as the predominant form in which lithocholic acid is found in tissue bound form.
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         Cholic Acid
         Chenodeoxycholic Acid
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         Glycocholic Acid
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         Medical Biochemistry
         Nutrition
         Medicinal Chemistry
         Microbial Genetics and Genomics
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