Interactions between Sodium Cholate or Sodium Deoxycholate and Nonionic Surfactant (Tween 20 or Tween 60) in Aqueous Solution

1. Adsorption of bile salts by dietary fibre is believed to promote their excretion and hence to reduce the serum cholesterol level in man and experimental animals.2. We have tested a number of plant fibre fractions and other related materials for their ability to adsorb bile salts from aqueous solution. The ‘insoluble’ plant fractions were from ‘dry grain’ (a residue from brewing), apple, wheat bran, lucerne (Medicago sativa), soya beans, mung beans (Phaseolus mungo), chick peas (Cicer arietinum), rolled oats, spinach (Spinacia oleracea), sunflower seeds, sawdust and sheep faeces. The other materials were cholestyramine, pectin and lignins prepared from wheat bran and from sawdust.3. Only cholestyramine and the fibre from lucerne, soya beans, mung beans, chick peas, spinach, and sunflower seeds adsorbed enough of either sodium cholate or sodium deoxycholate for adsorption to be detectable.4. This result conflicts with a report that the lignin component of dietary fibre is responsible for adsorption of bile salts.5. Adsorption of bile salts, when it occurs, may depend on the presence of saponins bound to the fibre.

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Laser light scattering and apparent molal volume studies on the association of sodium deoxycholate in aqueous solution

Journal de Chimie Physique ◽

10.1051/jcp/1984810393 ◽

1984 ◽

Vol 81 ◽

pp. 393-396 ◽

Cited By ~ 3

Author(s):

Dogan Emin Güveli

Keyword(s):

Aqueous Solution ◽

Light Scattering ◽

Laser Light ◽

Sodium Deoxycholate ◽

Laser Light Scattering ◽

Apparent Molal Volume ◽

Molal Volume

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Mucin biosynthesis. Properties of a bovine tracheal mucin β-6-N-acetylglucosaminyltransferase

Biochemical Journal ◽

10.1042/bj2270405 ◽

1985 ◽

Vol 227 (2) ◽

pp. 405-412 ◽

Cited By ~ 12

Author(s):

P W Cheng ◽

W E Wingert ◽

M R Little ◽

R Wei

Keyword(s):

Enzyme Activity ◽

Freezing Point ◽

Cetylpyridinium Chloride ◽

Sodium Dodecyl ◽

Sodium Deoxycholate ◽

Gas Chromatography Mass Spectrometry ◽

Tween 20 ◽

Group A ◽

Michaelis Constants ◽

Triton X

We have characterized a bovine tracheal mucin beta-6-N-acetylglucosaminyltransferase that catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to the C-6 of the N-acetylgalactosamine residue of galactosyl-β 1→3-N-acetylgalactosamine. Optimal enzyme activity was obtained between pH 7.5-8.5, at 5mM-MnCl2, and at 0.06-0.08% (v/v) Triton X-100 (or Nonidet P-40), or 0.5-5.0% (v/v) Tween 20. Ba2+, Mg2+ and Ca2+ could partially replace Mn2+, but Co2+, Fe2+, Cd2+ and Zn2+ could not. Sodium dodecyl sulphate, cetylpyridinium chloride, sodium deoxycholate, octyl beta-D-glucoside, digitonin and alkyl alcohols were less effective in enhancing enzyme activity, and dimethyl sulphoxide was ineffective. The apparent Michaelis constants were 1.25 mM for UDP-N-acetylglucosamine, 0.94-3.34 mM for freezing-point-depressing glycoprotein and 0.19 mM for periodate-treated blood-group-A porcine submaxillary mucin. Asialo ovine submaxillary mucin could not serve as the glycosyl acceptor. The structure of the 14C-labelled oligosaccharide obtained by alkaline-borohydride treatment of the product was identified as Gal beta 1→3(Glc-NAc beta 1→6)N-acetylgalactosaminitol by beta-hexosaminidase treatment, gas chromatography-mass spectrometry and 1H-n.m.r. (270 MHz) analysis. The enzyme is important in the regulation of mucin oligosaccharide biosynthesis.

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