Exploration of Interactions between Pyridoxine HCl (Vitamin B6) and {Hexadecyltrimethylammonium Bromide + Sodium Cholate (Trihydroxy Bile Salt)} Mixtures at T = (298.15 to 318.15) K: Physicochemical and Spectroscopic Approach

2021 ◽  
Author(s):  
Pallavi Sohal ◽  
Tarlok S. Banipal ◽  
Parampaul K. Banipal
Keyword(s):  
Bile Salt ◽  
Vitamin B6 ◽  
Sodium Cholate ◽  
Hexadecyltrimethylammonium Bromide ◽  
Salt Mixtures

Aggregation behaviour of amphiphilic drug and bile salt mixtures at different compositions and temperatures

2013 ◽  
Vol 64 ◽  
pp. 28-39 ◽  
Author(s):  
Malik Abdul Rub ◽  
Mohmad Shafi Sheikh ◽  
Abdullah M. Asiri ◽  
Naved Azum ◽  
Anish Khan ◽  
...  
Keyword(s):  
Bile Salt ◽  
Amphiphilic Drug ◽  
Aggregation Behaviour ◽  
Salt Mixtures

Comparison of In Vitro Binding of Bile Salt by Pectins from Various Sources

2012 ◽  
Vol 506 ◽  
pp. 274-277 ◽  
Author(s):  
K. Cheewatanakornkool ◽  
A. Chaidedgumjorn ◽  
U. Sotanaphun ◽  
S. Limsirichaikul ◽  
C. Wessapan ◽  
...  
Keyword(s):  
Bile Salt ◽  
Bile Salts ◽  
Serum Cholesterol Level ◽  
Sodium Deoxycholate ◽  
Sodium Cholate ◽  
Experimental Animals ◽  
Hypocholesterolemic Action ◽  
Acid Reaction ◽  
Layer Chromatography

Binding of bile salts by dietary fiber is believed to promote their excretion and hence to reduce the serum cholesterol level in man and experimental animals. In this study, the binding efficiency of soluble pectin from various sources, i.e., apple, citrus and pomelo, was examined. Sodium deoxycholate and sodium cholate hydrate were used as a model to represent bile salt in human body. The binding efficiency was assayed by acid reaction, thin layer chromatography (TLC) and enzyme cycling method. The results demonstrated that enzyme cycling method was the most suitable for assaying the in-vitro binding of bile salts while the TLC was not very sensitive, i.e., low amount of bile salts cannot be detected by TLC. Excess pectin from binding test could also interfere the acid reaction method even though the centrifugation was used to remove the excess pectin. When the concentration of pectin was increased, the binding efficiency with sodium deoxycholate increased. However, at 1% w/w of pectin, the binding efficiency decreased. The exception is for pomelo pectin in which the binding efficiency increased when the pectin concentration increased. With sodium cholate hydrate, only slight difference in binding efficiency was observed for all types and concentrations of pectin. The results indicate that the ability to bind bile salts of pectin might be responsible for its hypocholesterolemic action observed in experimental animals and humans.

Studies in Bile-Salt Solutions. XXII. The Effect of Reversed Micelles and of Aerosol-OT Aqueous Micelles on the Esterase Activity of Bile-Salt-Stimulated Human-Milk Lipase. Determination of Enzyme-Inhibitor Complex Dissociation Constants

1986 ◽  
Vol 39 (12) ◽  
pp. 2037 ◽  
Author(s):  
CJ Oconnor ◽  
IC Stockley ◽  
P Walde
Keyword(s):  
Human Milk ◽  
Bile Salt ◽  
Esterase Activity ◽  
Dissociation Constants ◽  
Sodium Taurocholate ◽  
Reaction Medium ◽  
Tris Buffer ◽  
Hexadecyltrimethylammonium Bromide ◽  
Aerosol Ot ◽  
Surfactant Complex

The esterase activity of bile-salt-stimulated human milk lipase has been measured against several 4-nitrophenyl alkanoate esters, including 4-nitrophenyl propionate, in reversed micellar solutions of several surfactants. The reaction media used were Aerosol-OT in isooctane, hexadecyltrimethylammonium bromide in chloroform/n-octane (1 : 1 v/v) or in chloroform, Triton X-100 in carbon tetrachloride or isooctane, lecithin in n-octane or diethyl ether/methanol (95 : 5 v/v) or benzene, and Brij 56 in cyclohexane . The reaction conditions varied over a range of cosolubilized water concentrations and initial pH values of added borate, glycine and Tris buffer solutions. In all cases decreased enzymic activity was observed, even if sodium taurocholate was present in the reaction medium. A detailed examination has been made on the effect of changing concentrations of 4-nitrophenyl propionate and of Aerosol-OT on the esterase activity of bile-salt-stimulated human milk lipase at 298 K in aqueous solutions of Tris buffer at pH 7.5. The inhibition induced by Aerosol-OT was identified as being reversible and mixed. The dissociation constants of the enzyme-surfactant complex and of the (enzyme-ester)-surfactant complex have been calculated to be equal to 0.125 and 0.48 mmol 1-1, respectively.

Multiple prototropism of fisetin in sodium cholate and related bile salt media

2011 ◽  
Vol 10 (1) ◽  
pp. 66-75 ◽  
Author(s):  
Susithra Selvam ◽  
Ashok K. Mishra
Keyword(s):  
Bile Salt ◽  
Sodium Cholate

Effects of hydrophobic and hydrophilic bile salt mixtures on cholesterol crystallization in model biles

2002 ◽  
Vol 1583 (2) ◽  
pp. 221-228 ◽  
Author(s):  
Niels G Venneman ◽  
Sebastiaan J Huisman ◽  
Antonio Moschetta ◽  
Gerard P vanBerge-Henegouwen ◽  
Karel J van Erpecum
Keyword(s):  
Bile Salt ◽  
Salt Mixtures

Form and structure of self-assembling particles in monoolein-bile salt mixtures

1995 ◽  
Vol 99 (44) ◽  
pp. 16395-16406 ◽  
Author(s):  
Rex P. Hjelm ◽  
Claudio Schteingart ◽  
Alan F. Hofmann ◽  
Devinderjit S. Sivia
Keyword(s):  
Bile Salt ◽  
Self Assembling ◽  
Salt Mixtures

scholarly journals Kinetics of the Micelle-to-Vesicle Transition: Aqueous Lecithin-Bile Salt Mixtures

2003 ◽  
Vol 85 (3) ◽  
pp. 1624-1646 ◽  
Author(s):  
J. Leng ◽  
S.U. Egelhaaf ◽  
M.E. Cates
Keyword(s):  
Bile Salt ◽  
Salt Mixtures ◽  
Kinetics Of

Studies in Bile Salt Solutions .XIII. Hydrophobic Substrate Effects on the Esterase Activity of Bile-Salt-Stimulated Human-Milk Lipase. Hydrolysis of 4-Nitrophenyl Alkanoates and Alkyl 4-Nitrobenzoates

1986 ◽  
Vol 39 (2) ◽  
pp. 249 ◽  
Author(s):  
CJ Oconnor ◽  
ASH Mitha ◽  
P Walde
Keyword(s):  
Human Milk ◽  
Bile Salt ◽  
Binding Site ◽  
Sodium Taurocholate ◽  
Sodium Cholate ◽  
Lipase Hydrolysis ◽  
Nitrobenzoic Acid ◽  
Hydrocarbon Chains ◽  
Hydrophobic Nature ◽  
Hydrolysis Of

The pseudo-first-order rate constants of hydrolysis of a series of 4-nitrophenyl alkanoates and a series of n-alkyl esters of 4-nitrobenzoic acid and of 4-nitrophenyl hexahydrobenzoate and cyclohexyl 4-nitrobenzoate, catalysed by bile-salt-stimulated human milk lipase in the absence and presence (2 mmol dm-3) of sodium cholate/cholic acid and sodium taurocholate , have been measured at pH 7.3, 310.5 K. It has been shown that the enzyme possesses a specific esterase acyl binding site which almost completely excludes the binding therein of a cyclohexyl group. There is also present a specific alkyl binding site which can fully accommodate a cyclohexyl ring. Both binding sites are hydrophobic in nature, but although the hydrophobic nature of the alkyl binding site is affected by bile-salt stimulation, that of the acyl site is not. Hydrophobicity parameters have been calculated for hydrocarbon chains lying in the acyl and alkyl binding positions of bile-salt-stimulated human milk lipase.

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