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Liver protein

K. Mizutani, T. Electronic and structural requirements for metabolic activation of butylated hydroxytoluene analogs to their quinone methides, intermediates responsible for lung toxicity in mice. Biol. Pharm. Bull. 1997, 20, 571-573. (c) McCracken, P. G. Bolton, J. L. Thatcher, G. R. J. Covalent modification of proteins and peptides by the quinone methide from 2-rm-butyl-4,6-dimethylphenol selectivity and reactivity with respect to competitive hydration. J. Org. Chem. 1997, 62, 1820-1825. (d) Reed, M. Thompson, D. C. Immunochemical visualization and identification of rat liver proteins adducted by 2,6-di- m-butyl-4-methylphenol (BHT). Chem. Res. Toxicol. 1997, 10, 1109-1117. (e) Lewis, M. A. Yoerg, D. G. Bolton, J. L. Thompson, J. Alkylation of 2 -deoxynucleosides and DNA by quinone methides derived from 2,6-di- m-butyl-4-methylphenol. Chem. Res. Toxicol. 1996, 9, 1368-1374. [Pg.85]

Reed, M. Thompson, D. C. Immunochemical visualization and identification of rat liver proteins adducted by 2,6-di-terf-butyl-4-methylphenol (BHT). Chem. Res. Toxicol. 1997, 10, 1109-1117. [Pg.353]

Liver toxicity, as evidenced by alterations in the incorporation of lysine into liver proteins, was observed in rats administered 192 mg lead/kg/day by gavage as lead acetate for 9 weeks (Barratt et al. 1989). No effects were observed at 21 mg lead/kg/day. However, the toxicological significance of this finding is not known because neither serum enzymes nor histopathological evaluations were performed. [Pg.180]

Steiner S et al. Protein variability in male and female Wistar rat liver proteins. Electrophoresis 1995 16 1969-1976. [Pg.122]

Anderson NL et al. An updated two-dimensional gel database of rat liver proteins useful in gene regulation and drug effect studies. Electrophoresis 1995 16 1977-1981. [Pg.123]

Anderson NL et al. Effects of toxic agents at the protein level quantitative measurement of 213 mouse liver proteins following xenobiotic treatment. [Pg.123]

Arce A et al. Changes in the liver protein pattern of female Wistar rats treated with the hypoglycaemic agent SDX PGU 693. Life Sci 1998 63 2243-2250. [Pg.123]

Giometti CS et al. A comparative study of the effects of clofibrate, ciprofibrate, WY14.643, and di-[2-ethylhexyl)-phthalate on liver protein expression in mice. Appl. Theoret Electrophoresis 1991 2 101-107. [Pg.123]

Fountoulakis M et al. Two-dimensional database of mouse liver proteins changes in hepatic protein levels following treatment with acetaminophen or its nontoxic regioisomer 3-acetamidophenol. Electrophoresis 2000 21 2148-2161. [Pg.123]

Newsholme SJ et al. Two-dimensional electrophoresis of liver proteins characterization of a drug-induced hepatomegaly in rats. Electrophoresis 2000 21 2122-2128. [Pg.124]

Duverger-van Bogaert M, Lambotte-Vandepaer M, Mercier M, et al. 1982a. In vitro covalent binding of acrylonitrile to rat liver proteins. Toxicol Lett 13 203-209. [Pg.101]

Anderson, N. L. et al., Simultaneous measurement of hundreds of liver proteins application in assessment of liver function, Toxicol. Pathol., 24, 72, 1996. [Pg.94]

Cessi, C., Columbini, C., and Mameli, L. 1966. The reaction of liver proteins with a metabolite of carbon tetrachloride. Biochem. J. 101 46-47c. [Pg.75]

Ritchie GP, Ho IK. 1982. Effects of chlordecone and mirex on amino acids incorporation into brain and liver proteins in the mouse. Neurotoxicology 3(4) 243-247. [Pg.281]

Robinson KM, Yarbrough JD. 1980. Liver protein synthesis and catabolism in mirex-pretreated rats with enlarging livers. J Pharmacol Exp Ther215(1) 82-85. [Pg.281]

Diet Liver Weight 3 Liver Protein Content Cytochrome... [Pg.393]

Fountoulakis, M., Bemdt, R, Boelsterli, U.S., Crameri, F., Winter, M., Albertini, S., and Suter, L., Two-dimensional database of mouse liver proteins changes in hepatic protein levels following treatment with acetaminophen or its nontoxic regioisomer 3-acetamidophenol, Electrophoresis 21, 2148-2161, 2000. [Pg.185]

Detection of liver injury has commonly been associated with alternations in serum levels of certain hepatic enzymes and proteins. Elevation in bilirubin levels following exposure (Barnes and Jones 1967) has been detected in humans, as have decreased serum levels of secreted liver proteins (e.g., albumin and fibrinogen) (Ashe and Sailer 1942 McGuire 1932 New et al. 1962 Norwood et al. 1950 Straus 1954). Elevations in serum levels of enzymes (e.g., ALT, AST, LDFI, OCT) have been reported following acute- and intermediate-duration exposures to carbon tetrachloride in animals (Bruckner et al. 1986 FI ayes et al. 1986 Sakata et al. 1987). [Pg.87]

Pharmacokinetics Rapidly absorbed from pulmonary, nasal, and G1 tissue. Undergoes extensive first-pass metabolism in the liver. Protein binding 87%. Primarily eliminated in feces. Half-life 15 hr... [Pg.120]

Well absorbed from the GI tract. Metabolized in the liver. Protein binding 30%. Primarily excreted in urine. Not removed by hemodialysis. Half-life 4-6 hr. [Pg.792]

Liver protein content Biochemical enzvme markers LivProt General condition Nutritional status Environmental pollutants Liver 6-15... [Pg.13]

It is reported that GPA-1734 inhibits prolyl and lysyl hydroxylations by Fe chelation and that the formation of non-dialyzable labeled hydroxyproline was inhibited 70% at a concentration of 50 pM, yet incorporation of proline into total liver protein was unaffected at this concentration (78BBA(538)328). GPA-1734 is a potent inhibitor of basement membrane synthesis (78MI21002). [Pg.570]

Small molecules are eliminated from the body largely by means of drug metabolism enzymes in the liver and other tissues and by urinary excretion. Large molecules are also eliminated by renal and hepatic mechanisms. Proteins that are less than 40 to 50 kDa are cleared by renal filtration with little or no tubular reabsorption. Larger proteins are less likely to be filtered but may be subject to phagocytosis in hepa-tocytes and Kupfer cells in the liver. Protein biotransformation—denaturation, proteolysis, and oxidative metabolism—is also important. [Pg.103]

Price et al. (1996) compared the toxicity of 0.5, 1 and 2 mmol/L coumarin in 24 h cultured precision-cut male Sprague-Dawley rat, Dunkin-Hartley guinea-pig, cyno-molgus monkey and human liver slices. Coumarin toxicity, based on liver protein synthesis and potassium content, was concentration-dependent in rat and guinea-pig liver, whereas monkey and human liver were relatively resistant. [Pg.212]

Chiang, R. W., Woolum, J. C., and Commoner, B. (1972). Further study on the properties of the rat liver protein involved in a paramagnetic complex in the livers of carcinogen-treated rats. Biochim. Biophys. Acta 257, 452-460. [Pg.165]


See other pages where Liver protein is mentioned: [Pg.367]    [Pg.72]    [Pg.28]    [Pg.425]    [Pg.347]    [Pg.766]    [Pg.1141]    [Pg.67]    [Pg.82]    [Pg.167]    [Pg.207]    [Pg.83]    [Pg.103]    [Pg.34]    [Pg.61]    [Pg.157]    [Pg.378]    [Pg.706]    [Pg.712]    [Pg.134]    [Pg.15]    [Pg.766]    [Pg.1141]    [Pg.297]    [Pg.902]   
See also in sourсe #XX -- [ Pg.211 ]

See also in sourсe #XX -- [ Pg.592 ]




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Fatty acid-binding proteins liver

Liver Protein turnover

Liver chronic disease, plasma protein

Liver disease protein synthesis alterations

Liver failure protein metabolism

Liver failure protein requirement

Liver metal/protein ratios

Liver microsomal protein

Liver plasma protein biosynthesis

Liver plasma protein synthesis

Liver protein oxidation

Liver protein synthesis

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Liver-type fatty acid-binding protein

Proteins Metabolism, Liver

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