scholarly journals The biochemical basis for the conjugation of bile acids with either glycine or taurine

1978 ◽  
Vol 174 (2) ◽  
pp. 621-626 ◽  
Author(s):  
Donald A. Vessey
Keyword(s):  
Guinea Pig ◽  
Bile Acids ◽  
Soluble Fraction ◽  
Rabbit Liver ◽  
Supernatant Fraction ◽  
Pig Liver ◽  
Biochemical Basis ◽  
High Affinity ◽  
Guinea Pig Liver ◽  
Soluble Fractions

All animals, except for the placental mammals, conjugate their bile acids exclusively with taurine. However, in certain of the placental mammals, glycine conjugates are also found. The basis for the appearance of glycine conjugation among the placental mammals was investigated. The reaction of choloyl-CoA with glycine and taurine, as catalysed by the soluble fraction from guinea-pig liver, had a high affinity for taurine and a poor affinity for glycine. The predominant synthesis of glycine conjugates in the guinea pig can be related to the fact that guinea-pig liver contains an unusually low concentration of taurine and a high concentration of glycine. Rabbits make exclusively glycine conjugates and their livers also contain low concentrations of taurine. However, the biochemical basis for their glycine conjugation is more straightforward than in the guinea pig in that the soluble fraction from rabbit liver has a high affinity for glycine and a poor affinity for taurine. Alternative-substrate-inhibition studies with glycine and taurine in soluble fractions from guinea-pig and rabbit liver revealed that glycine and taurine were mutually inhibitory. This suggests that there is only one enzyme for glycine and taurine conjugation in these tissues. The soluble fractions from bovine liver and human liver also made both glycine and taurine conjugates and evidence is presented that suggests that there is only one enzyme in these tissues too. Even the rat, which excretes mostly taurine conjugates, could make both glycine and taurine conjugates in vitro. However, in contrast with all of the placental mammals studied, the supernatant fraction from liver of the chicken, and other non-mammals, could not make glycine conjugates even in the presence of very high concentrations of glycine.

scholarly journals Purification and properties of a new testosterone 17β-dehydrogenase (NADP+) from guinea-pig liver

1977 ◽  
Vol 163 (3) ◽  
pp. 401-407 ◽  
Author(s):  
E Kaguera ◽  
S Toki
Keyword(s):  
Guinea Pig ◽  
Column Chromatography ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Supernatant Fraction ◽  
Pig Liver ◽  
Ring Junction ◽  
Purification And Properties ◽  
Androstane Derivatives ◽  
Guinea Pig Liver

As a result of studies of guinea-pig live testosterone 17beta-dehydrogenase (NADP+) (EC 1.1.1.64), a new testosterone 17beta-dehydrogenase was discovered. The new enzyme was purified to a single homogeneous protein from the 105 000 g-supernatant fraction of guinea-pig liver by (NH4)2SO4 fractional precipitation and two gel-filtration stages, DEAE-cellulose column chromatography and hydroxyapatite column chromatography. It was characterized by many properties. The enzyme has almost the same properties as the classical testosterone 17beta-dehydrogenase (NADP+) (EC 1.1.1.64), with respect to cofactor requirement, pH optima for dehydrogenation, effect of phosphate ion on the NAD+-dependent reaction and molecular weight, but characteristic differences were observed in substrate-specificity between the two dehydrogenases. With various androstane derivatives, the configuration of the A/B-ring junction was closely connected with enzyme activity. 5alpha-Androstanes, such as 5alpha-androstane-3alpha,17beta-diol, 5alpha-androstane-3beta,17beta-diol and 17beta-hydroxy-5alpha-androstan-3-one, and 5beta-congeners, such as 5beta-androstane-3alpha,17beta-diol, 5beta-androstane-3beta,17beta-diol and 17beta-hydroxy-5beta-androstan-3-one, served as substrates for both the EC 1.1.1.64 enzyme and the new enzyme. The EC 1.1.1.64 enzyme oxidized testosterone more rapidly than did the new enzyme. These comparisons were based on the relative activities, apparent Km values and apparent Vmax values.

scholarly journals Inhibition of glutathione S-transferase by bile acids

1981 ◽  
Vol 197 (2) ◽  
pp. 321-325 ◽  
Author(s):  
D A Vessey ◽  
D Zakim
Keyword(s):  
Bile Acid ◽  
Bile Acids ◽  
Soluble Fraction ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Pig Liver ◽  
Acceptor Substrate ◽  
Competitive Inhibitors ◽  
Guinea Pig Liver ◽  
Microsomal Glutathione

The effects of bile acids on the detoxification of compounds by glutathione conjugation have been investigated. Bile acids were found to inhibit the total soluble-fraction glutathione S-transferase activity from rat liver, as assayed with four different acceptor substrates. Dihydroxy bile acids were more inhibitory than trihydroxy bile acids, and conjugated bile acids were generally less inhibitory than the parent bile acid. At physiological concentrations of bile acid, the glutathione S-transferase activity in the soluble fraction was inhibited by nearly 50%. This indicates that the size of the hepatic pool of bile acids can influence the ability of the liver to detoxify electrophilic compounds. The A, B and C isoenzymes of glutathione S-transferase were isolated separately. Each was found to be inhibited by bile acids. Kinetic analysis of the inhibition revealed that the bile acids were not competitive inhibitors of either glutathione or acceptor substrate binding. The microsomal glutathione S-transferase from guinea-pig liver was also shown to be inhibited by bile acids. This inhibition, however, showed characteristics of a non-specific detergent-type inhibition.

Die Bedeutung der Homogenisationsart und -intensität für die Größe und Konstanz der Sauerstoffaufnahme von Meerschweinchen-Leberhomogenat / The Influence of Mode and Intensity of Homogenization on the Absolute Value and Stability of Oxygen Consumption of Guinea Pig Liver Homogenates

1977 ◽  
Vol 32 (11-12) ◽  
pp. 908-912 ◽  
Author(s):  
H. J. Schmidt ◽  
U. Schaum ◽  
J. P. Pichotka
Keyword(s):  
Oxygen Uptake ◽  
Guinea Pig ◽  
Measuring Time ◽  
Pig Liver ◽  
Absolute Value ◽  
Modified Method ◽  
Simultaneous Measurements ◽  
Liver Homogenates ◽  
The Absolute ◽  
Guinea Pig Liver

Abstract The influence of five different methods of homogenisation (1. The method according to Potter and Elvehjem, 2. A modification of this method called Potter S, 3. The method of Dounce, 4. Homogenisation by hypersonic waves and 5. Coarce-grained homogenisation with the “Mikro-fleischwolf”) on the absolute value and stability of oxygen uptake of guinea pig liver homogenates has been investigated in simultaneous measurements. All homogenates showed a characteristic fall of oxygen uptake during measuring time (3 hours). The modified method according to Potter and Elvehjem called Potter S showed reproducible results without any influence by homogenisation intensity.

Precision-cut Guinea-pig Liver Slices as a Tool for Studying the Toxicity of Volatile Anaesthetics

1990 ◽  
Vol 18 (1_part_1) ◽  
pp. 191-199
Author(s):  
Hanan N. Ghantous ◽  
Jeanne Fernando ◽  
Scott E. Morgan ◽  
A. Jay Gandolfi ◽  
Klaus Brandel
Keyword(s):  
Guinea Pig ◽  
Rank Order ◽  
Normal Liver ◽  
Liver Slice ◽  
Volatile Anaesthetics ◽  
Pig Liver ◽  
Liver Slices ◽  
Guinea Pig Liver ◽  
Krebs Henseleit Buffer

Cultured precision-cut liver slices retain normal liver architecture and physiological biochemical functions. Hartley male guinea-pig liver slices have proven to be a good model for studying the biotransformation and toxicity of halothane. This system was used to evaluate the biotransformation and toxicity of different volatile anaesthetics (halothane, enflurane, isoflurane and sevoflurane), and compare their effects to those of new anaesthetics (desflurane). Liver slices (250–300μm thick) were incubated in sealed roller vials, containing Krebs Henseleit buffer at 37°C under 95% O2:5% CO2 atmosphere. Volatile anaesthetics were delivered by volatilisation after pre-incubation for 1 hour to produce a constant concentration in the medium. Production of the metabolites, trifluroacetic acid and fluoride ion, was measured. Intracellular potassium ion content, protein synthesis and secretion were determined as indicators of viability of the slices. The rank order of biotransformation of anaesthetics by the liver slices was halothane >sevoflurane>isoflurane and enflurane>desflurane. The rank order of hepatotoxicity of these anaesthetics was halothane>isoflurane and enflurane>sevoflurane and desflurane. Halothane is the anaesthetic which is metabolised furthest and has the most toxic effect, while desflurane is the least metabolised anaesthetic and has the least toxicity. This in vitro cultured precision-cut liver slice system appears to be suitable for studying the biotransformation of volatile anaesthetics and correlating its role in the resulting toxicity.

scholarly journals Exolytic hydrolysis of toxic plant glucosides by guinea pig liver cytosolic beta-glucosidase.

1992 ◽  
Vol 267 (20) ◽  
pp. 14027-14032
Author(s):  
V Gopalan ◽  
A Pastuszyn ◽  
W R Galey ◽  
R.H. Glew
Keyword(s):  
Guinea Pig ◽  
Pig Liver ◽  
Beta Glucosidase ◽  
Toxic Plant ◽  
Hydrolysis Of ◽  
Guinea Pig Liver

scholarly journals THE REDUCTION OF l-XYLULOSE TO XYLITOL BY GUINEA PIG LIVER MITOCHONDRIA

1956 ◽  
Vol 221 (2) ◽  
pp. 697-709 ◽  
Author(s):  
Oscar Touster ◽  
V.H. Reynolds ◽  
Ruth M. Hutcheson
Keyword(s):  
Guinea Pig ◽  
Liver Mitochondria ◽  
Pig Liver ◽  
Guinea Pig Liver
Sign in / Sign up

Export Citation Format

Share Document