scholarly journals Comparative metabolism of mycophenolic acid by glucuronic acid and glucose conjugation in human, dog, and cat liver microsomes

2016 ◽  
Vol 40 (2) ◽  
pp. 123-129 ◽  
Author(s):  
J. E. Slovak ◽  
K. Mealey ◽  
M. H. Court
Keyword(s):  
Mycophenolic Acid ◽  
Glucuronic Acid ◽  
Liver Microsomes ◽  
Comparative Metabolism ◽  
Glucose Conjugation

Comparative metabolism of DDAO benzoate in liver microsomes from various species

2017 ◽  
Vol 44 ◽  
pp. 280-286 ◽  
Author(s):  
Hong-Ying Ma ◽  
Jia-Da Yang ◽  
Jie Hou ◽  
Li-Wei Zou ◽  
Qiang Jin ◽  
...  
Keyword(s):  
Liver Microsomes ◽  
Comparative Metabolism

A comparison of the in vitro metabolism of biphenyl and 4-chlorobiphenyl by rat liver microsomes

1978 ◽  
Vol 56 (10) ◽  
pp. 993-997 ◽  
Author(s):  
C. Wyndham ◽  
S. Safe
Keyword(s):  
Polychlorinated Biphenyl ◽  
Liver Microsomes ◽  
Low Molecular Weight ◽  
Rat Liver Microsomes ◽  
Hepatic Microsomes ◽  
Comparative Metabolism ◽  
Metabolic Products ◽  
Active Substrate ◽  
And Control

The comparative metabolism of the hydrocarbons, biphenyl and 4-chlorobiphenyl, was investigated using two different preparations of rat hepatic microsomes. The assay was designed to account for all the metabolic products which included the ether soluble lipophilic metabolites, low molecular weight conjugates, and macromolecular adducts, and to determine the effects of induction with Aroclor 1254 and 1248, two commercial polychlorinated biphenyl (PCB) preparations. 4-Chlorobiphenyl was the more metabolically active substrate with the induced and control enzymes. In most metabolic fractions biphenyl was less inducible by the PCB's, with the exception of the 2-biphenylol metabolite which was induced ca. 18-fold. Preincubation of the microsomes with carcinogens did not enhance biphenyl 2-hydroxylation. Instead, a general inhibition of metabolic activity was observed for both biphenyl and 4-chlorobiphenyl substrates. Preincubation with phenobarbitone, a noncarcinogen, did not change the microsome-mediated metabolism of biphenyl or 4-chlorobiphenyl. The substitution of a single halogen atom on the biphenyl nucleus altered both the reactivity and pattern of metabolites for these substrates.

Comparative metabolism of gelsenicine in liver microsomes from humans, pigs, goats and rats

2020 ◽  
Vol 34 (17) ◽  
Author(s):  
Zi‐Yuan Wang ◽  
Ming‐Ting Zuo ◽  
Xue‐Jiao Zhao ◽  
Yu‐Juan Li ◽  
Zhi‐Liang Sun ◽  
...  
Keyword(s):  
Liver Microsomes ◽  
Comparative Metabolism

Comparative metabolism of 7H-dibenzo[c,g]carbazole and dibenz[a,j]acridine by mouse and rat liver microsomes

1992 ◽  
Vol 81 (1-2) ◽  
pp. 131-147 ◽  
Author(s):  
Liping Wan ◽  
Weiling Xue ◽  
Joanne Schneider ◽  
Ray Reilman ◽  
Martha Radike ◽  
...  
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Comparative Metabolism

scholarly journals The effect of steroids and nucleotides on solubilized bilirubin uridine diphosphate glucuronyltransferase

1970 ◽  
Vol 119 (3) ◽  
pp. 437-445 ◽  
Author(s):  
B. P. F. Adlard ◽  
G. H. Lathe
Keyword(s):  
Enzyme Activity ◽  
Glucuronic Acid ◽  
Liver Microsomes ◽  
Fold Increase ◽  
Rat Liver Microsomes ◽  
Uridine Diphosphate ◽  
Competitive Effects ◽  
Solubilized Enzyme ◽  
High Concentrations ◽  
Solubilized Form

1. It was confirmed that bilirubin glucuronyltransferase can be obtained in solubilized form from rat liver microsomes. 2. Michaelis–Menten kinetics were not followed by the enzyme with bilirubin as substrate when the bilirubin/albumin ratio was varied. High concentrations of bilirubin were inhibitory. 3. The Km for UDP-glucuronic acid at the optimum bilirubin concentration was 0.46mm. 4. Low concentrations of Ca2+ were inhibitory in the absence of Mg2+ but stimulatory in its presence; the converse applied for EDTA. 5. UDP-N-acetylglucosamine and UDP-glucose enhanced conjugation by untreated, but not by solubilized microsomes. 6. The apparent 9.5-fold increase in activity after solubilization was probably due to the absence of UDP-glucuronic acid pyrophosphatase activity in the solubilized preparation. 7. The activation of solubilized enzyme activity by ATP was considered to be a result of chelation of inhibitory metal ions. 8. The solubilized enzyme activity was inhibited by UMP and UDP. The effect of UMP was not competitive with respect to UDP-glucuronic acid. 9. A number of steroids inhibited the solubilized enzyme activity. The competitive effects of stilboestrol, oestrone sulphate and 3β-hydroxyandrost-5-en-17-one, with respect to UDP-glucuronic acid, may be explained on an allosteric basis.

Comparative metabolism of benzo[ƒ]quinoline by liver microsomes from brown bullheads and rats

1989 ◽  
Vol 93 (2) ◽  
pp. 269-274 ◽  
Author(s):  
Chithan Kandaswami ◽  
Joel P. Rutkowski ◽  
Subodh Kumar ◽  
Harish C. Sikka
Keyword(s):  
Liver Microsomes ◽  
Comparative Metabolism

Comparative metabolism of benzo(a)pyrene, chrysene and phenanthrene by brown bullhead liver microsomes

1995 ◽  
Vol 39 (1-4) ◽  
pp. 51-55 ◽  
Author(s):  
Jyotsna Pangrekar ◽  
Chithan Kandaswami ◽  
Panna Kole ◽  
Subodh Kumar ◽  
Harish C. Sikka
Keyword(s):  
Liver Microsomes ◽  
Brown Bullhead ◽  
Comparative Metabolism
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