USE OF LIVER HOMOGENATES FOR STUDIES ON THE INTRACELLULAR SITE OF UBIQUINONE BIOSYNTHESIS

1966 ◽  
Vol 44 (12) ◽  
pp. 1615-1624 ◽  
Author(s):  
W. E. J. Phillips ◽  
M. Hidiroglou ◽  
G. Hatina

Mevalonic acid was incorporated into the ubiquinone and sterol fractions of rat-liver homogenates. The incorporation of mevalonate was increased approximately 10-fold in the total non-saponifiable matter including sterol by use of the in vitro homogenate system as compared with intact rats. The incorporation into the ubiquinones was decreased. The addition of potential ring precursors, p-hydroxybenzoic acid, L-phenylalanine, or L-tyrosine to the homogenate system did not increase incorporation of mevalonate into ubiquinone.Incubation of subcellular fractions from rat-liver homogenates demonstrated that supernate plus either mitochondria or microsomes were necessary for the biosynthesis of ubiquinone.

1960 ◽  
Vol 38 (10) ◽  
pp. 1105-1115 ◽  
Author(s):  
W. E. J. Phillips

Radioactive ubiquinone can be isolated from rat liver following intraperitoneal injections of C14-acetate or mevalonic acid. No detectable amount of radioactive ubiquinone could be isolated from liver homogenates, liver slices, or intestinal mucosa incubated in vitro with C14-acetate or mevalonic acid. The possible requirement of isolated tissues for an exogenous factor is discussed.


1960 ◽  
Vol 38 (1) ◽  
pp. 1105-1115 ◽  
Author(s):  
W. E. J. Phillips

Radioactive ubiquinone can be isolated from rat liver following intraperitoneal injections of C14-acetate or mevalonic acid. No detectable amount of radioactive ubiquinone could be isolated from liver homogenates, liver slices, or intestinal mucosa incubated in vitro with C14-acetate or mevalonic acid. The possible requirement of isolated tissues for an exogenous factor is discussed.


Life Sciences ◽  
1986 ◽  
Vol 38 (24) ◽  
pp. 2231-2238 ◽  
Author(s):  
Shinya Kobayshi ◽  
Yan Gao ◽  
Richard L. Ong ◽  
Constance S. Pittman

1977 ◽  
Vol 26 (11) ◽  
pp. 1043-1049 ◽  
Author(s):  
Ronald T. Coutts ◽  
Susan H. Kovach
Keyword(s):  

1978 ◽  
Vol 44 (1) ◽  
pp. 89-97 ◽  
Author(s):  
Paul J. Kostyniak ◽  
H. Bruce Bosmann ◽  
Frank A. Smith

2006 ◽  
Vol 3 (3) ◽  
pp. 329-338 ◽  
Author(s):  
Predrag Ljubuncic ◽  
Suha Dakwar ◽  
Irina Portnaya ◽  
Uri Cogan ◽  
Hassan Azaizeh ◽  
...  

Teucrium poliumL. (Lamiaceae) (RDC 1117) is a medicinal plant whose species have been used for over 2000 years in traditional medicine due to its diuretic, diaphoretic, tonic, antipyretic, antispasmodic and cholagogic properties. The therapeutic benefit of medicinal plants is often attributed to their antioxidant properties. We previously reported that an aqueous extract of the leaves and stems of this plant could inhibit iron-induced lipid peroxidation in rat liver homogenate at concentrations that were not toxic to cultured hepatic cells. Others have reported that organic extracts of the aerial components of this plant could inhibit oxidative processes. Against this background, we felt further investigation on the antioxidant action of the extract ofT. poliumprepared according to traditional Arab medicine was warranted. Accordingly, we assessed (i) its ability to inhibit (a) oxidation of β-carotene, (b) 2,2′-azobis(2-amidinopropan) dihydrochloride (AAPH)-induced plasma oxidation and (c) iron-induced lipid peroxidation in rat liver homogenates; (ii) to scavenge the superoxide ($${\hbox{ O }}_{2}^{\bullet -}$$) radical and the hydroxyl radical (OH•); (iii) its effects on the enzyme xanthine oxidase activity; (iv) its capacity to bind iron; and (v) its effect on cell glutathione (GSH) homeostasis in cultured Hep G2 cells. We found that the extract (i) inhibited (a) oxidation of β-carotene, (b) AAPH-induced plasma oxidation (c) Fe2+-induced lipid peroxidation in rat liver homogenates (IC50 = 7 ± 2 μg ml−1); (ii) scavenged $${\hbox{ O }}_{2}^{\bullet -}$$(IC50 = 12 ± 3 μg ml−1) and OH• (IC50 = 66 ± 20 μg ml−1); (iii) binds iron (IC50 = 79 ± 17 μg ml−1); and (iv) tended to increase intracellular GSH levels resulting in a decrease in the GSSG/GSH ratio. These results demonstrate that the extract prepared from theT. poliumpossesses antioxidant activityin vitro. Further investigations are needed to verify whether this antioxidant effect occursin vivo.


1986 ◽  
Vol 113 (2) ◽  
pp. 281-288 ◽  
Author(s):  
J. R. Saltzman ◽  
D. W. Clark ◽  
R. D. Utiger

Abstract. The liver is a major site of conversion of thyroxine (T4) to the more active thyroid hormone 3,5,3'-triiodothyronine (T3). Hepatic T4 to T3 conversion is altered by a variety of pathological processes and pharmacological agents. We studied T4 to T3 conversion in glucuronyl transferase deficient homozygous Gunn rats because they have a hepatic enzyme abnormality which leads to hyperbilirubinaemia, and also because they have been reported to have alterations in thyroid hormone metabolism. An in vitro incubation system employing the 10 000 × g supernatant of liver homogenate was used, and T3 production was measured by radioimmunoassay. Experiments were done using substrate concentrations ranging from 0.56 to 20 μm, tissue protein in concentrations ranging from 0.625 to 20 mg and incubation times of 15 to 60 min. T3 production by liver homogenates from homozygous Gunn rats in these studies ranged from 29 to 70% of that produced by liver homogenates from phenotypically normal heterozygous Gunn rats. The deficit in hepatic T3 production by homozygous rats could not be overcome by increasing cofactor concentrations. After ultracentrifugation at 100 000 μ g, T4-5'-deiodinase activity was found primarily in the 100 000 × g sediment fraction. Homogygous rat liver 100 000 × g sediment T3 production was 55% of that of the heterozygous rat liver 100 000 × g sediment. Liver cytosol from both homozygous and heterozygous rats inhibited microsomal T4-5'-deiodinase activity similarly. Addition of unconjugated bilirubin to liver homogenates resulted in reduction of T3 production in livers from both homozygous and heterozygous rats. Thus the diminished capacity for hepatic conversion of T4 to T3 in homozygous Gunn rats may be due to inhibition of T4-5'-deiodinase activity by high endogenous levels of unconjugated bilirubin.


1979 ◽  
Vol 177 (3) ◽  
pp. 993-995 ◽  
Author(s):  
E N Lalani ◽  
B Burchell

Addition of alkyl ketone (10mM) to Gunn-rat liver homogenates increased UDP-glucuronyltransferase activity towards 2-aminophenol by 10–20 fold, up to enhanced values of enzyme activity observed with similarly treated Wistar-rat liver homogenates. Alkyl ketones also activate the defective enzyme purified from Gunn-rat liver. This genetic deficiency of UDP-glucuronyltransferase activity is no longer apparent when assayed in the presence of alkyl ketones.


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