Bile Acid-binding Ability of Kaki-tannin from Young Fruits of Persimmon (Diospyros kaki) In Vitro and In Vivo

2010 ◽  
Vol 25 (4) ◽  
pp. 624-628 ◽  
Author(s):  
Kenji Matsumoto ◽  
Akio Kadowaki ◽  
Natsumi Ozaki ◽  
Makiko Takenaka ◽  
Hiroshi Ono ◽  
...  
Keyword(s):  
Bile Acid ◽  
Diospyros Kaki ◽  
Binding Ability ◽  
Bile Acid Binding

Effect of bile on the intestinal bile-acid binding protein (I-BABP) expression. In vitro and in vivo studies

FEBS Letters ◽  
1996 ◽  
Vol 384 (2) ◽  
pp. 131-134 ◽  
Author(s):  
T. Kanda ◽  
I. Niot ◽  
L. Foucaud ◽  
H. Fujii ◽  
A. Bernard ◽  
...  
Keyword(s):  
Bile Acid ◽  
Binding Protein ◽  
In Vivo Studies ◽  
Acid Binding Protein ◽  
Bile Acid Binding

Bile acid binding to dietary casein: A study in vitro and in vivo

1987 ◽  
Vol 73 (4) ◽  
pp. 343-350 ◽  
Author(s):  
A. Lanzini ◽  
W. J. F. Fitzpatrick ◽  
M. G. Pigozzi ◽  
T. C. Northfield
Keyword(s):  
Fatty Acid ◽  
Bile Acid ◽  
Aqueous Phase ◽  
Test Meal ◽  
Bile Acid Concentration ◽  
Ileal Resection ◽  
Lundh Test ◽  
Bile Acid Binding

1. Studies were carried out in vitro using an ultracentrifugation method to quantify bile acid binding to the different components of a Lundh test meal, and to determine what factors influence bile acid binding to one of the components (casein). We validated the ultracentrifugation method by showing good agreement with the equilibrium dialysis method. Studies were carried out in vivo on jejunal aspirate from 10 ileal resection patients in order to determine whether bile acid binding to casein could be demonstrated, and whether this influenced aqueous-phase bile acid and fatty acid concentrations. 2. In vitro, the Lundh test meal was found to adsorb bile acid. The protein content of the meal (casein) alone accounted for this binding, which was abolished by use of casein hydrolysate. The binding to casein was a saturable process. Both binding affinity and binding capacity were significantly greater for taurocholate at pH 4.5 than at pH 6.5, and for dihydroxylated than for trihydroxylated bile acid, suggesting that hydrophobic bonding was involved. 3. In vivo, jejunal samples aspirated at pH > 6 from 10 ileal resection patients showed 25% binding of bile acid to protein. On substitution of amino acids for casein, mean binding was reduced to 16% (P < 0.05), residual binding being attributed to endogenous protein. This was associated with an increase in fatty acid solubilization from 28% to 60% (P < 0.025). 4. These findings suggest that protein binding may have a critical effect on aqueous-phase bile acid and fatty acid concentrations in certain patients with a reduced total bile acid concentration as in ileectomy steatorrhoea, and in patients with defective lipolysis as in pancreatic insufficiency. This finding may provide an additional rationale for the use of elemental diets in severely ill patients with steatorrhoea.

Effect of bile and bile acids on binding of intrinsic factor to cobalamin and intrinsic factor-cobalamin complex to ileal receptor

1983 ◽  
Vol 245 (1) ◽  
pp. G72-G77
Author(s):  
B. Seetharam ◽  
M. Jimenez ◽  
D. H. Alpers
Keyword(s):  
Bile Acid ◽  
Bile Acids ◽  
Intrinsic Factor ◽  
Binding Ability ◽  
Human Bile ◽  
Receptor Molecule ◽  
Protease Digestion ◽  
Normal Absorption

Human bile or commercially available bile acids bind [57Co]cobalamin (Cbl) due to the presence of "R"-type binders, which are normally present in the former and present as a contaminant in the latter. The competition of these R proteins for the binding of Cbl by intrinsic factor (IF) could explain the in vivo inhibition attributed previously to the bile acids themselves. R protein seems to be involved in the inhibition of Cbl binding because protease digestion of either bile or bile acid abolishes the Cbl binding ability. Moreover, antibody to R protein abolishes the inhibition. Bile or bile acids do not have a direct effect on either purified IF or the IF-Cbl receptor molecule, even though bile acids increase the attachment of IF-[57Co]Cbl to ileal brush-border membranes. These data demonstrate two steps where components of bile could affect Cbl absorption: the binding of Cbl to IF and of IF-Cbl to its ileal receptor. It is not clear whether these in vitro phenomena are important for the normal absorption of Cbl in vivo.

Sign in / Sign up

Export Citation Format

Share Document