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1Author    Christian SteffenRequires cookie*
 Title    Absence of Microsomal Lipid Peroxidation in Acatalasemic Mice  
 Abstract    Catalase (E. C. activity and NADPH-depen-dent lipid peroxidation have been measured in liver micro­ somes from normal and acatalasemic mice. The absence of lipid peroxidation in acatalatic microsomes is not restituted by exogenous catalase as is microsomal methanol oxidation nor is it inhibited by sodium azide, thus suggesting an additional abnormality in these mice. 
  Reference    Z. Naturforsch. 34c, 301—303 (1979); received November 27 1978 
  Published    1979 
  Keywords    Acatalasemia, Microsomes, Lipid Peroxidation, Tissue Catalase, Catalase Inhibitors 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0301_n.pdf 
 Identifier    ZNC-1979-34c-0301_n 
 Volume    34 
2Author    DonaldE M Oreland, FrederickT. CorbinRequires cookie*
 Title    Influence of Safeners on the in vivo and in vitro Metabolism of Bentazon and Metolachlor by Grain Sorghum Shoots: a Preliminary Report  
 Abstract    Metabolism of bentazon and m etolachlor by excised shoots and a microsomal fraction iso­ lated from the shoots, of 3-day-old, dark-grown, grain sorghum (Sorghum bicolor cv. Funk G 522 DR) seedlings was studied. The effects of seed treatments, on the subsequent m etabo­ lism of the herbicides, with the safeners naphthalic anhydride, oxabetrinil, and CGA 133205 were compared against surface-sterilization and Captan-treatm ents. Bentazon was aryl hydroxylated in both in vivo and in vitro studies with the hydroxylated derivative undergoing glycosylation only under in vivo conditions. Both shoots and microsomes isolated from shoots of safener-treated seed showed enhanced metabolism of bentazon relative to the controls. In­ hibition by tetcyclacis, a potent inhibitor of plant cytochrome P-450 monooxygenases, in both the in vivo and in vitro studies, and a requirement for N A DPH in the in vitro studies suggested that the formation of hydroxybentazon was mediated by a cytochrome P-450 monooxygenase. Metolachlor was metabolized to polar material and O-desmethylmetolachlor under in vivo conditions. Only the demethylated product was formed in vitro. Shoots isolated from safener-treated seed showed enhanced form ation o f polar com pounds which were assumed to have arisen from conjugation with glutathione. Tetcyclacis did not affect the formation of the polar components. However, the form ation of O-desmethylmetolachlor was depressed in the shoots excised from safener-treated seed under both in vivo and in vitro conditions. Tetcyclacis com ­ pletely prevented form ation of the demethylated metabolite. Hence, formation of this m eta­ bolite is considered to be P-450 mediated. The differential response obtained with the safeners, i.e., stimulation of aryl hydroxylation o f bentazon and depression of metolachlor demethyla-tion, suggests that the reactions are probably catalyzed by different cytochrome P-450 m ono­ oxygenases. 
  Reference    Z. Naturforsch. 46c, 906—914 (1991); received M arch 26 1991 
  Published    1991 
  Keywords    Microsomes, Metolachlor, Bentazon, Cytochrome P-450, Mixed Function Oxidase 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0906.pdf 
 Identifier    ZNC-1991-46c-0906 
 Volume    46 
3Author    L. RaeymaekersRequires cookie*
 Title    The Sarcoplasmic Reticulum of Smooth M uscle Fibers  
 Abstract    The ability of the sarcoplasm ic (endoplasmic) reticulum (SR, ER) of smooth muscle cells to accumulate Ca was dem onstrated by measuring the uptake of 45Ca in fibers which were chemically skinned with saponin, and by electron cytochemistry of the accum ulated Ca. The Ca uptake was dependent on ATP and it was stim ulated by oxalate, as it is the case in SR of striated muscle. Electron microscopy of the skinned smooth muscle preparations revealed the presence o f calcium oxalate deposits in the reticulum . The SR vesicles were isolated from several sm ooth muscles. The purification was carried out by taking advantage o f the density increase o f the SR vesicles after loading with calcium in the presence of oxalate. Among the muscles investigated the smooth muscle of the pig stomach was found to be the most suitable and it was selected for further biochem ical and m orphological characterization of the SR vesicles. These vesicles, which contain calcium oxalate crystals, were able to accumulate an additional am ount of Ca. The Ca uptake was supported by several energy yielding substrates. T h eir order o f potency was ATP > dATP ~ U TP > ITP > G TP ~ CTP. The rate of Ca uptake was two orders o f m agnitude slower than that in SR of skeletal muscle. The measurement of the level o f phosphorylated Ca transport interm ediate showed that this difference is due to smaller num ber of calcium transport sites per vesicle. The distribution o f intram em ­ brane particles in freeze-fractured specimens is in agreem ent with this conclusion. 
  Reference    Z. Naturforsch. 37c, 481—488 (1982); received January 25 1982 
  Published    1982 
  Keywords    Smooth Muscle, Microsomes, Sarcoplasmic Reticulum, Calcium Metabolism, Electron Microscopy 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0481.pdf 
 Identifier    ZNC-1982-37c-0481 
 Volume    37 
4Author    DonaldE. Moreland, FrederickT. Corbin, WilliamP. Novitzky, CarolE. Parker, KennethB. TomerRequires cookie*
 Title    Metabolism of Metolachlor by a Microsomal Fraction Isolated from Grain Sorghum ( Sorghum bicolor) Shoots  
 Abstract    A microsomal fraction isolated from the shoots of 3-to 4-day-old, dark-grown, grain sor­ ghum (Sorghum bicolor cv. Funk G 522 D R) seedlings was characterized. The preparations had a cytochrome P-450 content that varied from approximately 90 to 150 pmol P-450/mg protein with cytochrome P-420 varying from 0 to 3% of the P-450 content. Type I difference spectra were formed with cinnamic acid and metolachlor, and a type II spectrum was formed with tetcyclacis. In short-term assays with [14C]metolachlor as substrate, the preparations produced a single time-dependent product that separated on silica gel TLC plates developed in benzene/ acetone (2:1, v/v). R F values for metolachlor and the metabolite were approximately 0.70 and 0.48, respectively. The microsomal reaction required N A D PH and oxygen, and was inhibited by carbon monoxide, with the inhibition being partially reversed by actinic light. Compounds known to inhibit the activity of cytochrome P-450 monooxygenases (piperonyl butoxide, tet­ cyclacis, and tridiphane) also prevented formation of the metabolite. Identity of the metabolite was confirmed by TLC and positive ion thermospray LC/MS to be 2-chloro-N-(2-ethyl-6-methylphenyl)-N-(2-hydroxy-l-methylethyl)acetamide. Hence, the reaction catalyzed by the sorghum microsomes involved O-demethylation of the methoxypropyl side chain of meto­ lachlor. 
  Reference    Z. Naturforsch. 45c, 558—564 (1990); received November 9 1989 
  Published    1990 
  Keywords    Microsomes, Metolachlor, Cytochrome P-450, Mixed Function Oxidase, Herbicide Metabolism 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0558.pdf 
 Identifier    ZNC-1990-45c-0558 
 Volume    45 
5Author    D. Onald, E. M. O Relan D, T. Hom, J. Fleischm, FrederickT C Orbina, JanisE M CfarlandbRequires cookie*
 Title    Differential Metabolism of the Sulfonylurea Herbicide Prosulfuron (CGA-152005) by Plant Microsomes  
 Abstract    Microsomes isolated from excised shoots of 3-day-old. dark grown, grain sorghum [Sor­ ghum bicolor (L.) Moench, Funk G522DR and DK 41Y] and corn seedlings [Zea mays (L.), Pioneer 3245] metabolized the sulfonylurea herbicide prosulfuron (CGA-152005). Corn microsomes predominantly formed a single major metabolite that resulted from hydroxyla-tion of the phenyl ring at the C5 position. However, sorghum microsomes formed two major metabolites in an approximate 1:1 ratio. One was the 5-hydroxyphenyl metabolite, whereas the second metabolite resulted from ö-demethylation at C4 of the triazine ring. Metabolite identity was established by mass spectrometry and co-chromatography with authentic stan­ dards. Metabolism in both corn and sorghum was greatly enhanced by pretreatment of the seed with naphthalic anhydride and by subirrigation with 2.5% ethanol 24 h prior to harvest. Metabolism required a reduced pyridine nucleotide and was affected by several cytochrome P450 monooxygenase inhibitors (carbon monoxide, tetcyclacis, piperonyl butoxide, 1 amino-benzotriazole, and SKF-525A). The inhibitors differentially affected metabolism of prosul­ furon. Microsomal oxidations from both untreated and inducer-treated tissue responded simi­ larly to the inhibitors. In exploratory studies, microsomes isolated from shoots of wheat [Triticum aestivum L., Pioneer 2548], barley [Hordeum vulgare L., Boone], oats [Avena sativa L., Southern States 76-30-P242] and rice [Oryza sativa L" Gulfmont], and room ripened avocado [Persea americana, Mill., Hass] mesocarp tissue also primarily formed the 5-hydroxy-phenyl metabolite. Titration of seven different avocado microsomal preparations with prosul­ furon provided typical type I difference spectra from which an average binding constant (/Cs) of 187 ± 35 [.im was obtained. Abbreviations: 1-ABT, 1-aminobenzotriazole; alachlor, 2-chloro-.'V-(2.6diethylphenyl)-/V-(methoxymethyl)acet-amide; ALS, acetolactate synthase; CG A 24704, 2-chloro-N-(2,6-dimethylphenyl)-/V-(2-methoxy-l-methylethyl)acet-amide; CGA-150829. 2-amino-4-methoxy-6-methyl-l,3,5-triazine; CGA-152005, prosulfuron, N-[[(4-methoxy-6-methyl-l,3,5-triazin-2-yl) amino]carbonyl]-2-(3,3,3-trifluoropropyl)benzenesulfonamide; CGA -l59902, 2-(3,3,3-tri-fluoropropyl)benzenesulfonamide; CGA-300406, 0-desmethyl prosulfuron, N[[(4-hydroxy-6-methyl-l,3,5-triazin-2-yl)amino]carbonyl]-2-(3,3,3-trifluoropropyl)benzenesulfonamide; CGA-300408, 5-hydroxy prosulfuron, N-[[(4me-thoxy-6-methyl-l,3,5-triazin-2-yl)amino]carbonyl]-2-(3,3,3-trifluoropropyI)-5-hydroxybenzenesulfonamide; chlorsul-furon, l-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3.5-triazin-2-yl)urea; pCMA, /?-chloro-./V-methylaniline: DMA, /V,/V-dimethylaniline; DMSO. dimethyl sulfoxide; DTT, dithiothreitol; G6P. glucose-6-phosphate; HPLC, high-performance liquid chromatography; LC/ESI/MS. liquid chromatography/ electrospray ionization/mass spectrome­ try; metolachlor, 2-chloro-/V-(2-ethyl-6-methylphenyl)-/V-(2-methoxy-l-methylethyl)acetamide; NA. 1,8-naphthalic anhydride; nicosulfuron, 2-[[(4.6-dimethoxypyrimidin-2-yl)aminocarbonyl]aminosulfonyl]-./V,/V-dimethyl-3-pyridinec-arboxamide; PBO. piperonyl butoxide; primisulfuron. 2-[[[[[4.6-bis(difluoromethoxy)-2pyrimidinyl]amino]carbony-l]amino]sulfonyl]benzoic acid: PVPP. polyvinylpolypyrrolidone; SKF-525A. 2-(diethylamino)ethyl-2.2-diphenylpen-tanoate; tetcyclacis, 5-(4-chlorophenyl)-3,4.5.9,10-pentaazatetracyclo[5.4.102-6,0811] dodeca-3.9-diene; TLC. thin layer chromatography: triasulfuron, l-(2-chloroethoxyphenylsulfonyl)-3-(6-methoxy-4-methyl-l,3.5-triazin-2-yl)urea. Reprint requests to Dr. D. E. Moreland. Telefax: (001) 919-515-7959. 0939-5075/96/0900-0698 $ 06.00 © 1996 Verlag der Zeitschrift für Naturforschung. All rights reserved. D D. E. Moreland et al. ■ M etabolism of Prosulfuron by Plant Microsomes 699 
  Reference    Z. Naturforsch. 51c, 698—710 (1996); received May 14/June 17 1996 
  Published    1996 
  Keywords    Microsomes, Prosulfuron, Cytochrome P450, Mixed Function Oxidases, Herbicide Metabolism 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0698.pdf 
 Identifier    ZNC-1996-51c-0698 
 Volume    51 
6Author    ZlatinaG. Naydenova3, KonstantinC. Grancharov3, DimitarK. Alargov3, EvgenyV. Golovinsky3, IvankaM. Stanoevab, LilianaD. Shalamanovab, IlzaK. PajevabRequires cookie*
 Title    Inhibition of UDP-glucuronosyltransferase by 5'-0-am ino Acid and Oligopeptide Derivatives of Uridine: Structure-Activity Relationships  
 Abstract    The inhibitory effect of a series of 5'-0-am ino acid and oligopeptide derivatives of uridine on rat liver UDP-glucuronosyltransferase (U G T) activities was investigated using two assay systems. A quantitative structure-activity relationship (Q SA R) study was performed. The compounds include a lipophilic residue linked to the nucleoside by a variable spacer. More­ over, half of the derivatives have two spacers linked to the uridine moiety. Compound 1, a serine derivative of isopropylideneuridine, was found to be the most potent inhibitor of both 4-nitrophenol (4-NP) and phenolphthalein (PPh) glucuronidation, with an I50 of 0.45 m M and 0.22 m M , respectively. Kinetic studies with this substance revealed a mixed type of inhibition towards 4-NP and UDP-glucuronic acid, with apparent Ki values of 150 ^ m and 120 (.i m , respectively. The dipeptide derivatives 11-14 exhibited a low activity against 4-NP conjuga­ tion. However, a marked suppression of PPh glucuronidation was found with compounds 11 and 13. Generally, compounds with two spacers are more inhibitory against the U G T activi­ ties studied. The Q SA R analysis outlined the significance of the spacers with a minimum length of 5 atoms and lipophilic residues linked to them for the inhibitory effect of the compounds. The most significant contribution to this effect is given by the six-atom spacer for both, 4-NP and PPh substrates. 4-NP converting U G T isoforms seem to respond more specifically to the inhibitors: a five-atom for the first and a six-atom for the second spacer enhance binding to both 4-NP and PPh conjugating isoenzymes, while a long second spacer contributes to inhibitor binding to U G T isoforms only converting PPh. 
  Reference    Z. Naturforsch. 53c, 173—181 (1998); received November 4 1997/January 14. 1998 
  Published    1998 
  Keywords    UDP-glucuronosyltransferase, Microsomes, Uridine Derivatives, Inhibitors, Q SA R 
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 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0173.pdf 
 Identifier    ZNC-1998-53c-0173 
 Volume    53