Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology最新文献

{"title":"Effect of the dietary brominated phenol, lanasol, on chemical biotransformation enzymes in the gumboot chiton Cryptochiton stelleri (Middendorf, 1846)","authors":"Bryan C. DeBusk ,&nbsp;Shukrit S. Chimote ,&nbsp;John M. Rimoldi ,&nbsp;Dan Schenk","doi":"10.1016/S0742-8413(00)00141-9","DOIUrl":"10.1016/S0742-8413(00)00141-9","url":null,"abstract":"<div><p>The effects of diet and other non-anthropogenic stressors on biochemical defenses and their relationship to susceptibility have been largely ignored in wildlife populations. Lanosol is a compound found in relatively high amounts in various marine species of Rhodophyta, including <em>Odonthalia dentata</em>. While previous studies demonstrated that lanosol is a feeding deterrent to several marine herbivores, <em>Cryptochiton stelleri</em> readily feeds upon <em>O. dentata</em>. To examine the effects of lanosol on the profile of biochemical defenses in <em>C. stelleri</em>, chitons were gavaged daily with 0, 1, 2.5, 5, or 10 mg/kg of lanosol. After three days of exposure, digestive gland microsomes were probed for expression of homologous isoforms of cytochromes P450 (CYP1A, CYP3A, and CYP2) and phase II enzymatic activities. Expression of a 43 kDa CYP3A-like protein was increased by approximately 45% over control following 2.5, 5, and 10 mg/kg treatments. Estradiol hydroxylase activity tended to increase with the dose of lanosol. UDP-glucuronosyl transferase activity was highly variable but appeared to increase at the two highest treatments, while sulfotranserase activity was significantly decreased at the three highest doses. Kinetic studies of GST activity showed lanosol is a non-competitive inhibitor of both CDNB and GSH in the GST-mediated conjugation reaction. These results show that dietary exposure to the brominated-phenol, lanosol, may alter expression and activity of some phase I and II biotransformation enzymes in chitons, potentially providing a dietary advantage for the species.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 2","pages":"Pages 133-142"},"PeriodicalIF":0.0,"publicationDate":"2000-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00141-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21907961","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inhibition of Na+,K+-ATPase in Penaeus indicus postlarvae by lead","authors":"Chinni Satyavathi,&nbsp;Yallapragada Prabhakara Rao","doi":"10.1016/S0742-8413(00)00130-4","DOIUrl":"10.1016/S0742-8413(00)00130-4","url":null,"abstract":"<div><p>The plasma membrane/mitochondrial fractions of <em>Penaeus indicus</em> postlarvae contain Mg²⁺-dependent ATPase, Na⁺,K⁺-stimulated ATPase, Na⁺-stimulated ATPase and K⁺-stimulated ATPase. The Na⁺,K⁺-activated, Mg²⁺-dependent ATPase was investigated further in relation to different pH and temperature conditions, and at various concentrations of protein, ouabain, ATP and ions in the incubation medium. In vitro and in vivo effects of lead were studied on the enzyme activity. In vitro lead inhibited the enzyme activity in a concentration-dependent manner with an IC₅₀ value of 204.4 μM. In correlation with in vitro studies, in vivo investigations (both concentration and time dependent) of lead also indicated a gradual inhibition in enzyme activity. A maximum decrease of 85.3% was observed at LC₅₀ (7.2 ppm) of lead for concentration-dependent experiments. In time-dependent studies, the decrease was maximal (81.7%) at 30 days of sublethal exposure (1.44 ppm). In addition, the substrate- and ion-dependent kinetics of Na⁺,K⁺-ATPase was studied in relation to in vitro exposure of lead; these studies suggest a non-competitive type of inhibition.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 11-22"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00130-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906692","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of ethoxyquin on the blood composition of turbot, Scophthalmus maximus L.","authors":"Tapati Bose Saxena ,&nbsp;Karl Erik Zachariassen ,&nbsp;Leif Jørgensen","doi":"10.1016/S0742-8413(00)00131-6","DOIUrl":"10.1016/S0742-8413(00)00131-6","url":null,"abstract":"<div><p>Ethoxyquin (6-ethoxy-2,2,4-trimethyl-1,2-dihydroquinoline (EQ) is a synthetic antioxidant used for preventing rancidity in animal foodstuffs. Three groups of ten fish were given a diet containing respectively 75 (control group with the commercial food), 200 and 400 ppm EQ for 16 days. The control group had a plasma osmolality and chloride concentration within the normal range of marine teleosts, but sodium concentrations of only about 110 mM, indicating the presence in the plasma of substantial amounts of another cation. Fish given food with 400 ppm EQ displayed a 70 mM increase in the plasma concentration of sodium. This indicates that EQ has disturbed the iono-regulatory mechanisms, probably by reducing the ATP production or inhibiting directly the Na/K-ATPase in the gills. The large increase in plasma sodium concentration was not accompanied by any significant increase in plasma osmolality, indicating that at least a part of the sodium added to the plasma is made osmotically inactive. In spite of the elevated plasma sodium concentration, the sodium content of erythrocytes of the 400-ppm EQ fish was reduced to half, while the content of calcium was unaffected. The transmembrane energy gradient of sodium in the EQ exposed turbot obviously increased, allowing them to use a sodium coupled antiport system to keep the cellular calcium content low when the Ca-ATPases blocked. A mechanism of this kind is also likely to be important to turbot that experience hypoxia under natural conditions. The 400-ppm group also displayed a substantial increase in liver weight, but the physiological significance of this effect is not clear. The leucocyte counts indicated the absence of obvious immunological effects.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 1-9"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00131-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Intraspecific variation in the venoms of the South American rattlesnake (Crotalus durissus terrificus)","authors":"Ivo M.B Francischetti ,&nbsp;Maria E.C Gombarovits ,&nbsp;Jesus G Valenzuela ,&nbsp;Célia R Carlini ,&nbsp;Jorge A Guimarães","doi":"10.1016/S0742-8413(00)00129-8","DOIUrl":"10.1016/S0742-8413(00)00129-8","url":null,"abstract":"<div><p>The venom of eight individual <em>Crotalus durissus terrificus</em> snakes from the State of Minas Gerais, Brazil, in addition to pooled venom from Butantan Institute, were compared. Snakes were captured in distinct locations, some of them 600 km apart: Conselheiro Lafaiete, Entre Rios de Minas, Itauna, Itapecerica, Lavras, Patos de Minas, Paracatu, and Santo Antonio do Amparo. The crude venoms were tested for proteolytic, phospholipase A2, platelet aggregating, and hemagglutinating activities. The venoms were also analyzed by polyacrylamide gel electrophoresis (PAGE) and isoelectric focusing (IEF). Chromatographic patterns of venom proteins on both gel-filtration and anion-exchange chromatographies were also performed. All venoms presented high phospholipase A2 and platelet-aggregating activities, but only minimal hemagglutinating or proteolytic activities were found. Gel-filtration chromatography showed a characteristic profile for most venoms where four main peaks were separated, including the typical ones where convulxin and crotoxin were identified; however, peaks with high amounts of lower molecular weight proteins were found in the venoms from the Santo Antonio do Amparo location and Butantan Institute, characterizing these venoms as crotamine positive. Anion-exchange chromatographies presented a similar protein distribution pattern, although the number of peaks (up to ten) distinguished some venom samples. Consistent with these results, polyacrylamide gels that were silver stained after venom separation by PAGE or IEF presented a similar qualitative band distribution, although a quantitative heterogeneity was detected among venoms. Our results suggest that the variability found in venom components of <em>C. d. terrificus</em> venoms captured in Minas Gerais State may be genetically inherited and/or environmentally induced.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 23-36"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00129-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906693","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Some aspects of hepatic function in feral brown trout, Salmo trutta, living in metal contaminated water","authors":"David O. Norris ,&nbsp;Jeanine M. Camp ,&nbsp;Tammy A. Maldonado ,&nbsp;John D. Woodling","doi":"10.1016/S0742-8413(00)00135-3","DOIUrl":"10.1016/S0742-8413(00)00135-3","url":null,"abstract":"<div><p>Brown trout, <em>Salmo trutta</em>, exposed to heavy metals (mainly Cd and Zn) for at least 2 years in the Eagle River, Colorado, were examined for liver size and activity of the growth-promoting enzyme, ornithine decarboxylase (ODC) and compared to trout living in an uncontaminated site. Liver-somatic index (LSI) was greater for trout living in the uncontaminated site with the LSI of females being significantly greater than that of males. The LSI for females at the uncontaminated site was greater than that of females at the contaminated site, but males were not different statistically. ODC activity in the livers of both males and females was lower at the contaminated site. However, males and females did not differ with respect to ODC activity. These data suggest that chronic exposure to heavy metals may have important implications for growth and reproduction and possibly survival. The activity of ODC in liver might serve as a useful biomarker when assessing chronic toxicity of metals to naturally reproducing fish populations.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 71-78"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00135-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906697","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heme oxygenase induction by menadione bisulfite adduct-generated oxidative stress in rat liver","authors":"Jorge O Ossola,&nbsp;Gisela Kristoff,&nbsp;Marı́a L Tomaro","doi":"10.1016/S0742-8413(00)00133-X","DOIUrl":"10.1016/S0742-8413(00)00133-X","url":null,"abstract":"<div><p>The in vivo effect of menadione bisulfite adduct on both hepatic oxidative stress and heme oxygenase induction was studied. A marked increase in lipid peroxidation was observed 1 h after menadione bisulfite adduct administration. To evaluate liver antioxidant enzymatic defenses, superoxide dismutase, catalase and glutathione peroxidase activities were determined. Antioxidant enzymes significantly decreased 3 h after menadione bisulfite adduct injection. Heme oxygenase activity appeared 6 h after treatment, peaking 9 h after menadione bisulfite adduct administration. Such induction was preceded by a decrease in the intrahepatic GSH pool and an increase in hydrogen peroxide steady-state concentration, both effects taking place some hours before induction of heme oxygenase. Iron ferritin levels and ferritin content began to increase 6 h after heme oxygenase induction, and these increases were significantly higher 15 h after treatment and remained high for at least 24 h after menadione bisulfite adduct injection. Administration of bilirubin entirely prevented heme oxygenase induction as well as the decrease in hepatic GSH and the increase in lipid peroxidation when administered 2 h before menadione bisulfite adduct treatment. These results indicate that the induction of heme oxygenase by menadione bisulfite adduct may be a general response to oxidant stress, by increasing bilirubin and ferritin levels and could therefore provide a major cellular defense mechanism against oxidative damage.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 91-99"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00133-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906554","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Catecholamines in larvae and juveniles of the prosobranch gastropod, Crepidula fornicata","authors":"Anthony Pires,&nbsp;Tonia R Guilbault ,&nbsp;Jeffrey V Mitten ,&nbsp;John A Skiendzielewski","doi":"10.1016/S0742-8413(00)00128-6","DOIUrl":"10.1016/S0742-8413(00)00128-6","url":null,"abstract":"<div><p>We investigated roles of catecholamines in metamorphosis of the prosobranch gastropod, <em>Crepidula fornicata</em>. Levels of DOPA, norepinephrine (NE) and dopamine (DA) were measured by high-pressure liquid chromatography (HPLC) in competent larvae and juvenile siblings that metamorphosed in response to the natural adult-derived cue or to elevated K⁺. Competent larvae contained 1.58±0.26 (S.E.M.)×10⁻² pmol DOPA, 0.91±0.45×10⁻² pmol NE, and 0.290±0.087 pmol DA (mean values per μg total protein, <em>n</em>=4 batches of larvae). Levels of DA per individual were not different between larvae and juvenile siblings; levels of NE were higher in juveniles. The tyrosine hydroxylase (TH) inhibitor α-methyl-<span>dl</span>-m-tyrosine (α-MMT) depleted DOPA and DA to approximately half of control values without affecting levels of NE. Depletion of DOPA and DA was accompanied by inhibition of metamorphosis in response to the natural cue but not to elevated K⁺. The dopamine-β-hydroxylase inhibitor diethyldithiocarbamate (DDTC) induced high frequencies of metamorphosis at concentrations of 0.1–10 μM. In juveniles induced by 10 μM DDTC, levels of both NE and DA averaged ∼80% of those in control larvae. Catecholamines may function as endogenous regulators of metamorphosis in <em>C. fornicata</em>.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 37-47"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00128-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906694","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Neurotensin elevates hepatic bile acid secretion in chickens by a mechanism requiring an intact enterohepatic circulation","authors":"Xianyong Gui ,&nbsp;Teresa F DeGolier ,&nbsp;Gary E Duke ,&nbsp;Robert E Carraway","doi":"10.1016/S0742-8413(00)00126-2","DOIUrl":"10.1016/S0742-8413(00)00126-2","url":null,"abstract":"<div><p>Neurotensin (NT), given intravenously at 10–50 pmol/kg per min to anesthetized female chickens equipped with a bile duct fistula, dose-dependently elevated hepatic bile flow and bile acid output but only when the enterohepatic circulation was maintained by returning the bile to the intestinal lumen. Infusion of NT at 10 and 50 pmol/kg per min increased the average hepatic bile acid output over a 30-min period to 138±11 and 188±13% of control, respectively. During infusion of NT, plasma levels of immunoreactive NT (iNT) increased in time from the basal level (14±1.3 pM) to reach steady state at 30 min. There was a near linear relationship between the dose of NT infused and the increment in plasma iNT. In addition, infusion of NT at 40 pmol/kg min gave a plasma level of iNT (≅88 pM) which was within the range of those observed during duodenal perfusion with lipid (54–300 pM) and near to that measured in hepatic portal blood from fed animals (52±5 pM). Perfusion of duodenum with lipid released endogenous NT and increased the rate of hepatic bile flow. When NT antagonist SR48692 was given, bile flow rate decreased to the basal level. These results suggest that intestinal NT, released by lipid, may participate in the regulation of hepatic bile acid output by a mechanism requiring an intact enterohepatic circulation.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 61-70"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00126-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906696","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of catecholamine depletion on oxidative energy metabolism in rat liver, brain and heart mitochondria; use of reserpine","authors":"Vaishali H. Shukla ,&nbsp;Kunjan R. Dave ,&nbsp;Surendra S. Katyare","doi":"10.1016/S0742-8413(00)00134-1","DOIUrl":"10.1016/S0742-8413(00)00134-1","url":null,"abstract":"<div><p>Regulation of mitochondrial functions in vivo by catecholamines was examined indirectly by depleting the catecholamines stores by reserpine treatments of the experimental animals. Reserpine treatment resulted in decreased respiratory activity in liver and brain mitochondria with the two NAD⁺-linked substrates: glutamate and pyruvate+malate with succinate ATP synthesis rate decreased in liver mitochondria only. With ascorbate+TMPD system, the ADP/O ratio and ADP phosphorylation rate decreased in brain mitochondria. For the heart mitochondria, state 3 respiration rates decreased for all substrates. In the liver mitochondria basal ATPase activity decreased by 51%, but in the presence of Mg²⁺ and/or DNP increased significantly. In the brain and heart mitochondria ATPase activities were unchanged. The energy of activation in high temperature range increased liver mitochondrial ATPase while in brain mitochondria reserpine treatment resulted in abolishment in phase transition. Total phospholipid (TPL) content of the brain mitochondria increased by 22%. For the heart mitochondria TPL content decreased by 19% and CHL content decreased by 34%. Tissue specific differential effects were observed for the mitochondrial phospholipid composition. Liver mitochondrial membranes were more fluidized in the reserpine-treated group. The epinephrine and norepinephrine contents in the adrenals decreased by 68 and 77% after reserpine treatment.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 79-90"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00134-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906698","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dietary vitamin-E modulates antioxidant defence system in giant freshwater prawn, Macrobrachium rosenbergii","authors":"Jagneshwar Dandapat ,&nbsp;Gagan B.N. Chainy ,&nbsp;K. Janardhana Rao","doi":"10.1016/S0742-8413(00)00132-8","DOIUrl":"10.1016/S0742-8413(00)00132-8","url":null,"abstract":"<div><p>The objectives of the present study were to determine the effect of supplementary vitamin-E (200, 400 and 600 mg/kg feed) on lipid peroxidation (LPX) and antioxidant defence system in gills and hepatopancreas of the freshwater prawn, <em>Macrobrachium rosenbergii</em>. Results indicated that vitamin-E inhibited LPX in the hepatopancreas in a comparatively lower dose than gills. Superoxide dismutase (SOD) activity was decreased significantly in gills in response to all the three supplemented diet, but in hepatopancreas decrease was observed only in response to higher doses of vitamin-E (400 and 600 mg/kg feed). Catalase (CAT) activity was reduced significantly only in gills but not in hepatopancreas. While glutathione peroxidase (GPX) activity was significantly elevated in the hepatopancreas by vitamin-E, its activity remains unaltered in gills. On the contrary, glutathione reductase (GR) activity was decreased in gills but that of hepatopancreas was constant. Glutathione (GSH) content of both gills and hepatopancreas was substantially elevated in the vitamin-E supplemented prawns. Although the ascorbic acid (ASA) content of gills was unchanged by vitamin-E, its level elevated significantly in hepatopancreas. Thus the findings of the present investigation suggest that dietary vitamin-E is capable of reducing LPX level and can modulate antioxidant defence system in gills and hepatopancreas, nevertheless, the response is highly tissue specific. It is further observed that highest dose of vitamin-E (600 mg/kg feed) could not render much additional protection in both the tissues.</p></div>","PeriodicalId":10586,"journal":{"name":"Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology","volume":"127 1","pages":"Pages 101-115"},"PeriodicalIF":0.0,"publicationDate":"2000-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0742-8413(00)00132-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21906555","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}