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1. 色素内視鏡検査 chromoendoscopy
2. 早産児における非経口栄養 parenteral nutrition in premature infants
3. 有機酸血症 organic acidemias
4. 血液-血液透析膜の相互作用に関与する生化学的機序 biochemical mechanisms involved in blood hemodialysis membrane interactions
5. 皮膚サルコイドーシスのマネージメント management of cutaneous sarcoidosis

English Journal

Cyclohexanecarboxyl-coenzyme A (CoA) and cyclohex-1-ene-1-carboxyl-CoA dehydrogenases, two enzymes involved in the fermentation of benzoate and crotonate in Syntrophus aciditrophicus.

Kung JW1, Seifert J, von Bergen M, Boll M.Author information 1Microbiology, Institute of Biology II, University of Freiburg, Freiburg im Breisgau, Germany.AbstractThe strictly anaerobic Syntrophus aciditrophicus is a fermenting deltaproteobacterium that is able to degrade benzoate or crotonate in the presence and in the absence of a hydrogen-consuming partner. During growth in pure culture, both substrates are dismutated to acetate and cyclohexane carboxylate. In this work, the unknown enzymes involved in the late steps of cyclohexane carboxylate formation were studied. Using enzyme assays monitoring the oxidative direction, a cyclohex-1-ene-1-carboxyl-CoA (Ch1CoA)-forming cyclohexanecarboxyl-CoA (ChCoA) dehydrogenase was purified and characterized from S. aciditrophicus and after heterologous expression of its gene in Escherichia coli. In addition, a cyclohexa-1,5-diene-1-carboxyl-CoA (Ch1,5CoA)-forming Ch1CoA dehydrogenase was characterized after purification of the heterologously expressed gene. Both enzymes had a native molecular mass of 150 kDa and were composed of a single, 40- to 45-kDa subunit; both contained flavin adenine dinucleotide (FAD) as a cofactor. While the ChCoA dehydrogenase was competitively inhibited by Ch1CoA in the oxidative direction, Ch1CoA dehydrogenase further converted the product Ch1,5CoA to benzoyl-CoA. The results obtained suggest that Ch1,5CoA is a common intermediate in benzoate and crotonate fermentation that serves as an electron-accepting substrate for the two consecutively operating acyl-CoA dehydrogenases characterized in this work. In the case of benzoate fermentation, Ch1,5CoA is formed by a class II benzoyl-CoA reductase; in the case of crotonate fermentation, Ch1,5CoA is formed by reversing the reactions of the benzoyl-CoA degradation pathway that are also employed during the oxidative (degradative) branch of benzoate fermentation.
Journal of bacteriology.J Bacteriol.2013 Jul;195(14):3193-200. doi: 10.1128/JB.00322-13. Epub 2013 May 10.
The strictly anaerobic Syntrophus aciditrophicus is a fermenting deltaproteobacterium that is able to degrade benzoate or crotonate in the presence and in the absence of a hydrogen-consuming partner. During growth in pure culture, both substrates are dismutated to acetate and cyclohexane carboxylate
PMID 23667239

How can Faecalibacterium prausnitzii employ riboflavin for extracellular electron transfer?

Khan MT1, Browne WR, van Dijl JM, Harmsen HJ.Author information 1Department of Medical Microbiology, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.AbstractFaecalibacterium prausnitzii is one of the most abundant commensal microbes in the human gut. It is an important supplier of butyrate to the colonic epithelium, and low numbers of faecalibacteria have been associated with severe inflammatory bowel disease. Previous studies revealed that F. prausnitzii shuttles electrons extracellularly to oxygen in systems containing flavins and thiols. Since this electron shuttling to oxygen strongly stimulates growth, the present studies were aimed at elucidating the role of riboflavin as an extracellular electronophore of F. prausnitzii. We show that F. prausnitzii can use riboflavin as a mediator for extracellular electron transfer (EET) to the anode of microbial fuel cell systems. However, this bacterium relies on exogenous riboflavin, since it does not secrete this compound as shown by the analysis of a spent growth medium using cyclic voltammetry (CV). Importantly, CV showed that riboflavin can undergo fully reversible redox cycling under physiologically relevant conditions. Lastly, riboflavin is shown to mediate the electrochemical oxidation of the main bacterial reducing equivalent NADH. Based on our present observations, we hypothesize that riboflavin is of major importance as a redox mediator for bacterial EET and growth in the human gut.
Antioxidants & redox signaling.Antioxid Redox Signal.2012 Nov 15;17(10):1433-40. doi: 10.1089/ars.2012.4701. Epub 2012 Jun 25.
Faecalibacterium prausnitzii is one of the most abundant commensal microbes in the human gut. It is an important supplier of butyrate to the colonic epithelium, and low numbers of faecalibacteria have been associated with severe inflammatory bowel disease. Previous studies revealed that F. prausnitz
PMID 22607129

Interactions of acidic pharmaceuticals with human serum albumin: insights into the molecular toxicity of emerging pollutants.

Chen J1, Zhou X, Zhang Y, Qian Y, Gao H.Author information 1Key Laboratory of Yangtze River Water Environment for Ministry of Education, College of Environmental Science and Engineering, Tongji University, Shanghai, 200092, China.AbstractAcidic pharmaceuticals such as diclofenac (DCF), clofibric acid (CA) and ketoprofen (KTP) have been detected frequently in environmental media. In order to reveal the toxicity of such emerging pollutants, their interactions with human serum albumin (HSA) were investigated by capillary electrophoresis, molecular spectrometry, and equilibrium dialysis. The binding constants and sites of these acidic pharmaceuticals with HSA were obtained. The thermodynamic parameters, e.g. enthalpy change and entropy change of these interactions were calculated to characterize that all the reactions resulted from hydrophobic and electrostatic interactions. The static quenching of the fluorescence of HSA was observed when interacted with acidic pharmaceuticals, indicating acidic pharmaceuticals bound to Tryptophan residue of HSA. The 3D fluorescence and circular dichroism confirmed that the secondary conformation of HSA changed after the interactions with the pharmaceuticals. At physiological condition, only 0.12 mM acidic pharmaceuticals reduced the binding of vitamin B(2) to HSA by 37, 30 and 21% for DCF, KTP and CA, respectively. This work provides an insight into non-covalent interactions between emerging contaminants and biomolecule, and is helpful for clarifying the toxic mechanism of such emerging contaminants.
Amino acids.Amino Acids.2012 Oct;43(4):1419-29. Epub 2012 Feb 4.
Acidic pharmaceuticals such as diclofenac (DCF), clofibric acid (CA) and ketoprofen (KTP) have been detected frequently in environmental media. In order to reveal the toxicity of such emerging pollutants, their interactions with human serum albumin (HSA) were investigated by capillary electrophoresi
PMID 22307229

Japanese Journal

難水溶性製剤の溶出試験に界面活性剤として使用されるポリソルベート80の品質に関する研究

梶村計志,川口正美,四方田千佳子
医薬品医療機器レギュラトリーサイエンス 43(7), 650-655, 2012
NAID 40019383655

皮膚疾患におけるビタミンＥとＢ２の配合剤および単味剤の臨床効果の検討

BES研究班
皮膚 31(6), 856-881, 1989
酢酸d-α-トコフェロール100mgとビタミンB2酪酸エステル20mgの配合剤 (EとB2), E単味剤 (E), B2単味剤 (B2) の皮膚疾患における臨床効果を検討した。アトピー性皮膚炎, 乾燥性湿疹を対象とし …
NAID 130004897555

Effect of riboflavin-butyrate on cardiac glutathione reductase affected by adriamycin.

日野雄二,YOO Seung Boo,梶山公則,鍵山明弘,小倉良平
Journal of Nutritional Science and Vitaminology 31(2), 139-145, 1985
… Male Wistar rats received intraperitoneal injections of adriamycin (4mg/kg body weight/day) and/or riboflavin-butyrate (20mg/kg body weight/day) for 6 consecutive days. … The combined use of riboflavin-butyrate with adriamycin was evaluated for reduction of lipid peroxide formation in rat cardiac mitochondria. …
NAID 130001371139