Figure 3a,b shows room-temperature luminescence spectra for the Z

Figure 3a,b shows room-temperature luminescence spectra for the ZnO-nanorod-based heterojunction without and with NiO buffer layer, respectively. It can be seen that a small peak at 425 nm is originating from the GaN substrate; however, a weak UV peak and a wide broad peak in the visible regions are also observed as shown in Figure 3a. Using the NiO buffer layer, the luminescence

DihydrotestosteroneDHT solubility dmso properties of the n-type ZnO nanorods/learn more p-type GaN heterojunction are highly improved as shown in Figure 3b. The used NiO buffer layer has enhanced the luminescence properties due to more favourable hole injections and double recombination compared to the heterojunction without NiO buffer layer. It can be observed that the accelerating voltage has also made an influence on the local luminescence properties of the fabricated heterojunctions. The measured spectra showed that the number of excited carriers seems in proportion with the accelerating voltage. Similarly, ZnO-nanotube-based heterojunctions

were developed without and with NiO buffer layer on the GaN substrate, and the luminescence behaviour was studied by the CL technique as shown in Figure 3c,d, respectively. It can be observed that Cediranib mw the NiO buffer layer has also shown the same luminescence trend as in the case of the ZnO nanorods. Figure 3 CL spectra of nanorods and nanotubes without and with NiO buffer layer. ZnO nanorods (a) on GaN and (b) on NiO thin-layer-coated GaN. ZnO nanotubes

(c) on GaN and (d) on NiO thin-layer-coated on GaN. Figure 4 shows the CL spectra for the comparative study of nanorods and nanotubes based on devices at a fixed voltage of 20 kV. It can be clearly seen that the NiO has significantly contributed for the enhanced luminescent performance of the prepared light-emitting diodes compared to the light-emitting diode without a NiO buffer layer. Figure 4 Comparative CL spectra of ZnO nanorods and nanotubes with and without buffer layer. (a) CL spectra of ZnO nanorods (b) CL spectra of ZnO nanotubes. The room temperature EL of the fabricated LEDs under forward bias at a constant current of 15 mA is shown in Figure 5. Figure 5a shows the EL response Isotretinoin for the n-type ZnO nanorods/p-type GaN-developed LED in the presence and absence of the NiO buffer layer. In addition to the fabrication of NiO-buffer-layer-based LEDs with ZnO nanorods, the ZnO-nanotube-based LEDs were also produced. The EL spectra are shown in Figure 5b. It can be inferred that by introducing the NiO buffer layer, the luminescence properties of LEDs are significantly improved due to more injection holes, and a large number of electron-hole recombination is taking place at the interface.

J Clin Chem Clin Biochem 1978,16(9):533–534 PubMed 46 Gerova M,

J Clin Chem Clin Biochem 1978,16(9):533–534.PubMed 46. Gerova M, Halgasova N, Ugorcakova J, Bukovska G: Endolysin of bacteriophage

BFK20: PX-478 price evidence of a catalytic and a cell wall binding domain. FEMS Microbiol Lett 2011,321(2):83–91.PubMedCrossRef Competing interests The authors have no competing interests to declare. Authors’ contributions YHY and QP conducted the protein analysis. YHY performed the bioinformatics buy GSK3326595 analyses. MYG supervised the work. MYG and YHY designed the study and wrote the manuscript. All authors reviewed and approved the final version of the manuscript.”
“Background DNA vaccination has gained a lot of attention since its ability to induce long-lasting humoral and cellular immune responses against an encoded antigen was discovered [1]. In addition, DNA vaccination poses no danger of integration into host cellular DNA thereby raising its safety profile [2–4]. DNA vaccines can be easily isolated to high purity, encode multiple

antigens, and possess inherent adjuvant activity due to the presence of unmethylated CpG motifs that are recognized in mammals by TLR9 [5]. So called purified “Naked” DNA vaccination was shown to be highly efficient in rodents and mice, but not in larger animals and humans [6]. Consequently, it is very important to optimize DNA vaccine vectors and develop a delivery system to facilitate cellular uptake and enhance gene transfer efficiency and expression in situ[7]. Several strategies have been explored to protect plasmids from this website degradation, facilitating DNA uptake by phagocytic Antigen Presenting Cells (APCs) and thereby enhancing their immunological properties. This includes delivery technologies based on encapsulation into synthetic particles (cationic liposomes or polymers) or the use of viral vectors [7, 8]. Despite their potential, some limitations and safety issues still remain which can restrict the application of gene therapy – e.g. the complexity of producing liposomes and their limited packaging capacity

[9]. Additionally, it was shown that some viral vectors have the capacity to randomly integrate their genetic material into the host genome causing insertional mutagenesis of a cellular oncogene, leading 5-Fluoracil to tumour formation [10]. The use of bacteria as delivery vehicles for DNA vaccination has emerged as an interesting alternative to overcome many of the problems associated with viral or liposomal delivery [11]. W. Schaffner was the first to observe genetic material transfer from bacteria to mammalian cells [12]. Since then, bacteria have been extensively exploited as vaccine delivery vehicles for vaccination against bacterial and viral pathogens as well as cancer immunotherapy [13–15]. The use of bacteria for mucosal delivery of DNA vaccines may be advantageous due to their potential to elicit secretory IgA responses as well as systemic immunity, when compared to conventional parenteral immunization [16].

References 1 Ruud JS: Nutrition and the Female Athlete Nutrition

References 1. Ruud JS: Nutrition and the Female Athlete Nutrition. Consultant Lincoln Nebraska: CRC Press; 1996. 2. Jacqueline RB: Nutrition for Exercise and Sports Performance. In Krause’s Food, Nutrition and Therapy. 10th edition. Edited by: L Kathleen Mahan, Sylvia Escott-Stump. Pub WB. Saunders Company; 2000:535. 3. Jeukendrup AE, Gleeson M: Sport Nutrition: An Introduction to Energy Production and Performance. Human Kinetix; 2004. 4. Kearney JM, McElhone S: Perceived barriers in trying to eat healthier-results of a pan-EU consumer attitudional survey. British Journal of Nutrition 1999,81(2):133–137.CrossRef 5.

Cotugna N, Vickery CE, McBee S: Sports Nutrition for Young Athletes. The Journal of School Nursing 2005,21(6):323–328.CrossRef 6. Yılmaz E, Özkan S: Üniversite öğrencilerinin beslenme alışkanlıklarının incelenmesi. Fırat Sağlık #check details randurls[1|1|,|CHEM1|]# Hizmetleri Dergisi 2007,2(6):87–104. 7. Rosenbloom CA, Jonnalagadda SS, Skinner R: Nutrition knowledge of collegiate athletes in a division I national

collegiate Athletic Association Institution. Journal of the American Dietetic Association 2002,102(3):418–420.PubMedCrossRef 8. Zawila LG, Steib CSM, Hoogenboom B: The female collegiate cross-country runner, nutritional knowledge and attitudes. Journal of Athletic Training 2003,38(1):67–74.PubMed 9. Rastmanesh R, Taleban FA, Kimiagar M, Mehrabi Y, Salehi M: Nutritional knowledge and attitudes in athletes DAPT solubility dmso with physical disabilities. Journal of

Athletic Training 2007,42(1):99–105.PubMed 10. Juzwiak CR, Ancona-Lopez F: Evaluation of nutrition knowledge and dietary recommendations by coaches Selleck CBL-0137 of adolescent Brazilian athletes. Int J Sport Nutr Exerc Metab 2004, 14:222–235.PubMed 11. Ersoy G: Egzersiz ve spor yapanlar için beslenme. Ankara: Nobel Yayın Dağıtım; 2004. 12. Kalpakçıoğlu BB: Nutrition in Sportsmen. Rheumatism 2008, 23:24–27. 13. Clark N: Nancy Clark’s Sports Nutrition Guidebook. 3rd edition. Champaign IL: Human Kinetics; 2003. 14. Position of Dietitians of Canada, the American Dietetic Association, and the American College of Sports Medicine: endorsed by the Coaching Association of Canada Can J Diet Prac Res 2000, 61:176–192. 15. Lemon PWR: Effects of exercise on dietary protein requirements. International Journal of Sports Nutrition 1998,8(4):426–477. 16. Jacobson BH, Aldana SG: Current nutrition practice and knowledge of varsity athletes. The Journal of Strength and Conditioning Research 1992,6(4):232–238. 17. Yeung DL, Laquatra I: HEINZ Handbook of nutirition. United States. 9th edition. H.J. Heinz Company; 2003. 18. Position of the American Dietetic Association, Dietitians of Canada, and the American College of Sports Medicine. Nutrition and athletic performance Journal of the American Dietetic Association 2000,100(12):1543–1556. 19. Lutz CA, Przytulski KR: Nutrition and diet theraphy. Third edition. Philadelphia, F.A.

Further research may be directed at determining the optimum dose

Further research may be directed at determining the optimum dose of PS to achieve favorable

endocrine response in athletes. Acknowledgements The authors would like to thank Chemi Nutra, 4463 White Bear Pkwy, Suite 105, White Bear Lake, MN 55110, USA, for assistance with funding of this project and publication of this manuscript. This study was partially funded by a Research Enhancement Grant from West Texas A&M University. References 1. Jäger R, Purpura M, Kingsley M: Phospholipids and sports performance. J Int Soc Sports Nutr 2007, 4:5.PubMedCrossRef 2. Crook TH, Tinklenberg J, Yesavage J, Petrie W, Nunzi MG, Massari DC: Effects of phosphatidylserine in age-associated memory impairment. Neurol 1991,41(5):644–649. 3. Kingsley M: Effects of phosphatidylserine supplementation on exercising humans. Sports Med 2006,36(8):657–669.PubMedCrossRef 4. Starks GSK458 supplier MA, Starks SL, Kingsley M, Purpura M, Jäger R: The effects of phosphatidylserine on endocrine response to moderate intensity exercise. J Int Soc Sports Nutr 2008.,5(11): 5. Jäger R, Purpura M, Geiss K-R, Weiß M, Baumeister J, Amatulli F, Schröder L, Herwegen H: The effect of phosphatidylserine on golf performance. J Int Soc Sports Nutr 2007, 4:23.PubMedCrossRef 6. Baumeister J, Barthel T, Geiss KR,

Weiss M: Influence of phosphatidylserine on cognitive performance and cortical activity after LY294002 in vivo induced stress. Nutritional Neuroscience 2008,11(3):103–110.PubMedCrossRef 7. Scholey AB, French SJ, Morris PJ, Kennedy DO, Milne AL, Haskell CF: Consumption of cocoa flavanols results in acute improvements in mood and cognitive performance during selleck kinase inhibitor sustained mental effort. [http://​jop.​sagepub.​com/​content/​early/​2009/​11/​26/​0269881109106923​] Journal of Psychopharmacology 2009. 8. Martin DT, Andersen MB, Gates W: Using Profile of Mood States

(POMS) to monitor high-intensity training in cyclists: group versus case studies. The Sport PsychologistP 2000, 14:138–156. 9. Benton D, Donohoe RT, Sillance B, Nabb S: The influence of phosphatidylserine supplementation on mood and heart rate when faced with an acute stressor. Nutr Neurosci 2001,4(3):169–178.PubMed 10. Hellhammer J, Fries E, Buss C, Engert V, Tuch A, Rutenberg D, Hellhammer D: Effects of soy lecithin phosphatidic acid and phosphatidylserine complex (PAS) on the endocrine and psychological responses to mental stress. Stress 2004,7(2):119–126.PubMedCrossRef mafosfamide 11. Monteleone P, Maj M, Beinat L, Natale M, Kemali D: Blunting by chronic phosphatidylserine administration of the stress induced activation of the hypothalamo-pituitary-adrenal axis in healthy men. Eur J Clin Pharmacol 1992, 42:385–388.PubMed 12. Kinglsey MI, Wadsworth D, Kilduff LP, McEneny J, Benton D: Effects of phosphatidylserine on oxidative stress following intermittent running. Med Sci Sports Exerc 2005,37(8):1300–6.CrossRef 13. Kinglsey MI, Miller M, Kilduff LP, McEneny J, Benton D: Effects of phosphatidylserine on exercise capacity during cycling in active males.

Reversible addition-fragmentation chain transfer (RAFT) polymeriz

Reversible addition-fragmentation chain transfer (RAFT) polymerization was used to synthesize the pDEAEA following a published procedure (Figure  1, step 3) [18, 23]. The resulting polymer had a molecular weight of 4,380 g/mol as determined by GPC. This polymer was deposited on the external surface of the pSi rugate

filter by spin coating (Figure  1, step 4), in a manner that the polymer acts as a barrier to prevent the ingress of water into the porous matrix.In order to test the reliability of using the optical properties of pSi rugate filters and the penetration of the polymer inside the pores, the white-light reflectance SAR302503 cell line spectrum from the pDEAEA-covered pSi

film modified with silane was recorded and compared with the silane-functionalized pSi film without polymer. The spectrum obtained from the silanized pSi displays a sharp resonance at a wavelength of 540.0 nm (Figure  2a, trace A). Figure  2a (trace B) shows the reflectance spectrum at the same spot after spin coating of the polymer. The rugate peak is observed at a wavelength of 541.8 nm, very similar to the resonance observed for the control, therefore confirming that the polymer has not penetrated into the pores to a significant extent. The intensity of the reflectance spectrum of the sample high throughput screening modified with pDEAEA is slightly smaller (~1.3 times smaller) than the one observed for the control. Had the pores been filled with polymer during spin coating, the resonance peak would be expected to red shift by approximately 111 nm according to a simulation using the transfer matrix method. We conclude from these observations that the presence of the second pDEAEA does not obstruct the optical spectrum of the pSi reflector. In addition, the lack of

a significant change in the wavelength of the rugate peak before and after the polymer layer deposition confirms that pDEAEA does not infiltrate the porous layer. Figure 1 Fabrication of pSi-pDEAEA composite films. A piece of flat silicon is subjected to electrochemical etching using HF as an electrolyte followed by (1) thermal oxidation, (2) the oxidized pSi film is functionalized with the silane, (3) the DEAEA monomer is subjected to RAFT polymerization reaction, and (4) the pDEAEA is spin-coated onto the surface. Figure 2 Reflectance spectra of the oxidized pSi surface and FTIR-ATR spectra for pSi samples. (a) Reflectance spectra of the oxidized pSi surface modified with silane (A) and of the pSi after spin coating of pDEAEA (B). (b) FTIR-ATR spectra for pSi samples modified with silane (A) and with a layer of pDEAEA spin-coated on the surface (B). The spectra were baseline-corrected.

The fact that low expression of the klotho gene occurs in tissues

The fact that low expression of the klotho gene occurs in tissues other than the kidney and brain, including the pituitary, placenta, skeletal muscle, urinary bladder, aorta, pancreas, testis, ovary, thyroid gland, and colon, does not necessarily negate the concept that the Klotho detected in the peritoneal dialysate originates, at least in part, from several tissues near the peritoneum [1]. Although no data were available regarding the relationship between the peritoneal Klotho and IgG levels among our subjects, the positive relationship between the amount of peritoneal Klotho and the concentrations of total protein and albumin in the effluent

MRT67307 dialysate demonstrated in the present study, and the previous findings that the molecular weight of the soluble form of Klotho is estimated to be 130 kDa [11], seem to support the concept that there might be no local Klotho production in the peritoneum, and that the peritoneal soluble Klotho detected in the present study may therefore have originated

from the serum, thereby modulating the serum level of soluble Klotho in the PD subjects. On the other hand, the urinary excreted Klotho detected in our subjects may not have been of glomerular origin, but rather, may have originated exclusively from the renal tubules, because we failed to confirm any significant associations Selleckchem IWP-2 between the amounts of urinary excreted Klotho and those Amino acid of albumin and total protein, despite the significant correlation between the urinary total protein and albumin. Given that urinary soluble Klotho is of glomerular origin, the renal kinetics of albumin might be comparable to those of urinary soluble Klotho, because the molecular weight of soluble Klotho is approximately twofold that of albumin [11, 24]. There is still insufficient evidence to explain our finding of an undetectable level of

peritoneal Klotho in one PD subject. However, it is reasonable to consider that the presence of an undetermined neutralizing factor or inhibitor of Klotho might have been involved. Otherwise, differences in peritoneal permeability may play a role in the presence or absence of Klotho in the peritoneal dialysate. Indeed, the majority of our patients with detectable peritoneal Klotho were categorized as high average transporters by a peritoneal equilibration test, while the selleck chemical patient with undetectable Klotho was categorized as a low transporter (data not shown). Consequently, the clinical impact of the serum level of soluble Klotho should be evaluated carefully, especially among PD patients. Although the present study provided new information on the kinetics of soluble Klotho among PD subjects, our results should be interpreted within the context of the study limitations.

3) CcmL and CsoS4A have been structurally characterized (Tanaka

3). CcmL and CsoS4A have been structurally characterized (Tanaka et al. 2008); both form pentamers and have a pronounced concave/convex sidedness similar to the hexamers. In contrast to the hexameric shell proteins, the electrostatic potential of these proteins is predominantly

positive (Fig. 6). The structures of CcmL and CsoS4A can be superimposed with an RMSD of 0.74 Å over 58 C-α atoms. The largest difference between the primary structures of these two proteins is in the region corresponding to an 8–10 amino acid loop on the concave face of the pentamer that seems to influence the charge of the concave face. A similar difference is seen between the paralogs CsoS4A and CsoS4B. In this region CsoS4B has more positively MK5108 datasheet charged residues than CsoS4A. The pores Based on the current models of mTOR inhibitor carboxysome function and structure, pores in the shell protein hexamers provide conduits for the flux of metabolites; bicarbonate ions and RuBP diffuse in and 3PGA to diffuses out, while preventing the BTSA1 order leakage of CO2 from the interior (Dou et al. 2008). The shell also prevents oxygen from diffusing in, reducing unwanted photorespiration by RuBisCO (Marcus et al. 1992). As the shell localizes CA and RuBisCO together, the overall rate of CO2 fixation by RuBisCO is enhanced; effectively, the carboxysome provides a focal point for the carbon concentrating mechanism (CCM) (Fig. 2). A key characteristic of carboxysome shell proteins is a narrow (~4–7 Å

diameter; Kerfeld et al. 2005) central pore that is formed at the 5- and 6-fold axis of symmetry by a loop in the hexamers and pentamers, respectively. Residues forming this loop tend to be conserved

among paralogs; for example, these residues are K-I-G-S and R-(A/V)-G-S in CcmK2 and CcmK4, respectively (Table 1). Such differences in residues flanking the pore likely Protein kinase N1 influence the flux of metabolites into or out of the carboxysome by influencing the size and charge of the pore. All of the pores of structurally characterized carboxysome shell proteins are positively charged at the narrowest point (Fig. 9); presumably this provides a favorable attractive force for negatively charged metabolites such as bicarbonate. At the same time, a charged pore would not attract molecules lacking a dipole moment, such as CO2 and oxygen (Fig. 9). Table 1 List of structurally characterized BMC-domain proteins from the carboxysome and their dimensions Pfam00936 protein Carboxysome type Hexamer diameterb (Å) Hexamer edge lengthc (Å) Pore residues Pore diameter (Å) CsoS1A [2G13] α 72 36 FVGG 4 CsoS1C [3H8Y] α 72 36 FVGG 4 CcmK1 [3BN4] β 75 37 KIGS 4.8 (5.5) CcmK2 [2A1B] β 75 35 KIGS 5.5 (7) CcmK4 [2A10] β 75 37 RAGS 4 CsoS1Da [3F56] α 72 36 ERAF 12.5 (14) PDB IDs of the listed structures are in brackets. aCsoS1D is a tandem BMC-domain protein; values for the dimensions of the pseudohexamer are reported. b Hexamer diameter was measured from one vertex to its opposite vertex.

PubMedCrossRef 23 André T, Boni C, Mounedji-Boudiaf

L, N

PubMedCrossRef 23. André T, Boni C, Mounedji-Boudiaf

L, Navarro M, Tabernero J, Hickish T, Topham C, Zaninelli M, Clingan P, Bridgewater J, Tabah-Fisch I, de Gramont A: Oxaliplatin, fluorouracil, and leucovorin as adjuvant treatment for colon cancer. N Engl J Med 2004,350(23):2343–2351.PubMedCrossRef 24. Thorsteinsson MKL, Lund LR, Sørensen LT, Gerds TA, Jess P, Olsen J: Gene expression profiles in stage II and III colon cancer. Application of a 128-gene signature. Int J Colorectal Dis 2012,27(12):1579–1586.PubMedCrossRef 25. Smith JJ, Deane NG, Wu F, Merchant NB, Zhang B, Jiang A, Lu P, Johnson JC, Schmidt C, Bailey CE, Eschrich S, Kis C, Levy S, Washington MK, Heslin MJ, Coffey RJ, Yeatman TJ, Shyr Y, Beauchamp RD: Experimentally derived metastasis gene expression profile predicts recurrence and death in patients with colon cancer. Gastroenterology 2010,138(3):958–968.PubMedCentralPubMedCrossRef click here 26. Staub E, Groene J, Heinze M, Mennerich D, Caspase inhibitor Roepcke S, Klaman I, Hinzmann B, Castanos-Velez E, Pilarsky C, Mann B, Brümmendorf T, Weber B, Buhr HJ, Rosenthal A: An expression module of WIPF1-coexpressed genes identifies patients with favorable prognosis in three tumor types. J Mol Med (Berl) 2009,87(6):633–644.CrossRef 27.

de Sousa E Melo F, Colak S, Buikhuisen J, Koster J, Cameron K, de Jong JH, Tuynman JB, Prasetyanti PR, Fessler E, van den Bergh SP, Rodermond H, Dekker E, van der LY2090314 cell line Loos CM, Pals ST, van de Vijver MJ, Versteeg R, Richel DJ, Vermeulen L, Medema JP: Methylation of cancer-stem-cell-associated Wnt target genes predicts poor prognosis in colorectal cancer patients. Cell Stem Cell 2011,9(5):476–485.PubMedCrossRef 28. Reid JF, Gariboldi M, Sokolova V, Capobianco P, Lampis A, Perrone F, Signoroni S, Costa A, Leo E, Pilotti S, Pierotti MA: Integrative approach for prioritizing cancer genes in sporadic colon cancer. Genes Chromosomes Cancer 2009,48(11):953–962.PubMedCrossRef 29. Kaiser S, Park YK, Franklin JL, Halberg RB, Dolichyl-phosphate-mannose-protein mannosyltransferase Yu M, Jessen WJ, Freudenberg J, Chen X, Haigis K, Jegga AG, Kong S, Sakthivel B, Xu H, Reichling T, Azhar M, Boivin GP, Roberts RB, Bissahoyo AC, Gonzales F, Bloom GC, Eschrich S, Carter SL, Aronow JE, Kleimeyer J, Kleimeyer M, Ramaswamy V, Settle

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The most recent advisory committee meeting, which dealt with the

The most recent advisory committee meeting, which dealt with the issue of adult acetaminophen overdose, was conducted in 2009 and formed the basis for current decisions that are being made by the FDA and industry about

how to dose acetaminophen in both nonprescription and prescription products.[9] To address the issues surrounding acetaminophen toxicity, the FDA Center for Drug Evaluation and Research (CDER) prepared an internal report that formed the basis for discussion at the 2009 advisory committee meeting. The committee members were asked to vote upon several recommendations, which included reducing the total daily acetaminophen dose from 4000 mg to 3250 mg, limiting tablet strength EGFR assay to 325 mg/tablet, and switching the 500 mg strength to prescription status.[9] The advisory GSK2126458 manufacturer committee was generally sympathetic to these interventions as ways to reduce acetaminophen toxicity.[9] As with all

advisory committees, the committee was purely ‘advisory’ to the FDA, and its recommendations were not binding to the FDA. However, the recommendations of the CDER group and the advisory committee and subsequent actions by the FDA and voluntary actions by industry have created significant confusion about the Selleck INK-128 therapeutic or ‘proper’ dose of acetaminophen. What is the maximum safe daily dose of acetaminophen? In reality, the FDA has never validated the threshold toxic dose for the average adult. The 3900 mg maximum daily dose, as recommended originally, was deemed to be safe and is five to seven times lower than the estimated median lethal dose (LD50) of 400 mg/kg. The 1977 panel used anecdotal reports suggesting that 15 g was the hepatotoxic dose; therefore, a dose of 650 mg was 23 times less than the hepatotoxic dose. Subsequently, the analgesic monograph dictated that 3900–4000 mg was a safe and effective maximum daily dose if acetaminophen

was used properly and according to the approved labeling. History has demonstrated the safety of this dose. In 1994, Whitcomb and Block published the results of their retrospective case series review of 126 779 hospital discharge summaries from the University of Pittsburgh Medical Center to identify those patients who were taking acetaminophen and who developed severe hepatotoxicity.[10] from Forty-nine patients with severe acetaminophen-induced hepatotoxicity (defined as an aspartate aminotransaminase level >1000 U/L) were identified: 28 patients had an intentional acetaminophen overdose, and 21 were taking acetaminophen for therapeutic reasons. All of these patients had taken more than the recommended daily maximum dose of 4000 mg. No hepatotoxicity was identified in patients who had therapeutic doses of acetaminophen or less than 4000 mg/day. A prospective study by den Hertog and colleagues evaluated the use of acetaminophen in 697 stroke patients who received a dose of 6000 mg daily for 3 days. None of the patients had liver enzyme changes.

Appl Environ Microbiol 2003, 69:4343–4351 PubMedCrossRef 10 Ster

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