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1994[X]
61Author    Barbara TimmermannRequires cookie*
 Title    External Flavonoids in Two Grindelia Species  
  Reference    Z. Naturforsch. 49c, 395 (1994) 
  Published    1994 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0395_n.pdf 
 Identifier    ZNC-1994-49c-0395_n 
 Volume    49 
62Author    N. Onaki Tanno, Masayoshi Nakayama3, Hirofumi Yashima, Kyoshi Sunaga, Mamoru Abe, Nobuo Okagamib, Takao YokotaaRequires cookie*
 Title    Gibberellins A 19 and A24 from Yams, Dioscorea bulbifera, D. pentaphylla and D. oppositifolia  
 Abstract    Gibberellin A 19 (G A 19) and G A 24 were identified by gas chromatography-mass spec­ trometry from growing shoots o f four strains of three species o f D ioscorea, D. bulbifera var. vera, D. pentaphylla and D. oppositifolia (yams), which are distributed in the subtropical and tropical regions of Asia. An earlier report indicated the presence of several G A s including G A !9 and G A 24 in a cultivated temperate species of East Asia, D. opposita; these findings suggest possible coexistence of two G A biosynthetic pathways, early 13-hydroxylation and non-13-hydroxylation pathways comm only in Asian species of Dioscorea. 
  Reference    Z. Naturforsch. 49c, 399 (1994); received April 22 1994 
  Published    1994 
  Keywords    Dioscorea, Gibberellins, Shoots, Yams 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0399.pdf 
 Identifier    ZNC-1994-49c-0399 
 Volume    49 
63Author    L.Ömtir DemirezerRequires cookie*
 Title    Concentrations of Anthraquinone Glycosides of Rumex crispus during Different Vegetation Stages  
 Abstract    The anthraquinone glycoside contents of various parts of Rumex crispus L. (Polygonaceae) in different vegetation stages were investigated by thin layer chromatographic and spectro-photometric methods. The data showed that the percentage o f anthraquinone glycoside in all parts of plant increased at each stage. Anthraquinone glycoside content was increased in leaf, stem, fruit and root from 0.05 to 0.40%. from 0.03 to 0.46%. from 0.08 to 0.34%, and from 0.35 to 0.91% respectively. From the roots of R. crispus, em odin-8-glucoside, RGA (isolated in our laboratory, its structure was not elucidated), traceable amount of glucofran-gulin B and an unknown glycoside (R f = 0.28 in ethyl acetate:m ethanol:w ater/100:20:10) was detected in which the concentration was increased from May to August. The other parts of plant contained only emodin-8-glucoside. 
  Reference    Z. Naturforsch. 49c, 404 (1994); received January 31 1994 
  Published    1994 
  Keywords    Rumex crispus, Polygonaceae Anthraquinone, Glycoside 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0404.pdf 
 Identifier    ZNC-1994-49c-0404 
 Volume    49 
64Author    Thomas Huff, Hans-Georg Kuball, Timm AnkeRequires cookie*
 Title    7-Chloro-4,6-dimethoxy-l(3H)-isobenzofurane and Basidalin: Antibiotic Secondary Metabolites from Leucoagaricus cameifolia Gillet (Basidiomycetes)  
 Abstract    7-Chloro-4,6-dim ethoxy-l(3H)-isobenzofurane, Basidalin, Leucoagaricus cameifolia, Basidiomycete, Antibiotic Two antibiotic m etabolites were isolated from cultures of Leucoagaricus cameifolia. Their structures were elucidated by spectroscopic methods. The first compound, 7-chloro-4,6-di-m ethoxy-l(3 H)-isobenzofurane (1) had to our knowledge not been described from natural sources whereas the second, basidalin (2), is a known m etabolite o f L. naucina (H. Iinuma et al., 1983). 1 exhibits antibiotic activities with minimal inhibitory concentrations of 20 ^g/ml against Botrytis cinerea, the most sensitive microorganism. 
  Reference    Z. Naturforsch. 49c, 407 (1994); received April 4 1994 
  Published    1994 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0407.pdf 
 Identifier    ZNC-1994-49c-0407 
 Volume    49 
65Author    A. Kio Kobayashi, Yutaka Koguchi, Hiroshi Kanzaki, Shin-Ichiro Kajiyama, Kazuyoshi KawazuRequires cookie*
 Title    A New Type of Antimicrobial Phenolics Produced by Plant Peroxidase and Its Possible Role in the Chemical Defense Systems against Plant Pathogens  
 Abstract    Syringaldehyde readily reacted in the horse-radish peroxidase (H R P O D) system. The ethyl acetate extract of the reaction mixture showed a marked antimicrobial activity against bac­ teria and fungi. A fter repeated column chromatography three potential antimicrobial com ­ pounds were obtained from the extract. The structural elucidation of active compounds was achieved by a combination of spectroscopic techniques and chemical modification. 
  Reference    Z. Naturforsch. 49c, 411 (1994); received January 1/April 25 1994 
  Published    1994 
  Keywords    Peroxidase, Syringaldehyde, Phenolics, Antimicrobial Compounds, Chemical D efense System 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0411.pdf 
 Identifier    ZNC-1994-49c-0411 
 Volume    49 
66Author    Xiangbo Kang, H.Ekkehard Neuhaus, Renate ScheibeRequires cookie*
 Title    Subcellular Localization of Quinate: Oxidoreductase from Phaseolus mungo L. Sprouts  
 Abstract    Quinate:oxidoreductase (Q O R ase, EC 1.1.1.24) was isolated and purified from etiolated mung bean (Phaseolus mungo L.) sprouts and a m onospecific antiserum was raised in rabbit to the hom ogeneous protein. Highly intact etioplasts were isolated from the same plant material. The stroma o f the purified etioplasts was enzymatically characterized. Contami­ nation by cytosol, mitochondria and vacuole was estimated from activities of marker en­ zymes. QO Rase activity was localized in the stroma (about 91% for both N A D + and N A D P + as a cofactor). Western blotting and immunoprinting o f the stroma proteins revealed a single band that migrated identically with the purified QO Rase. The results suggest that the Q O R ­ ase is localized predominantly, if not exclusively, in the etioplast stroma. The physiological role of the enzyme is discussed. 
  Reference    Z. Naturforsch. 49c, 415 (1994); received March 24/April 27 1994 
  Published    1994 
  Keywords    Phaseolus mungo, Q uinate:O xidoreductase, Quinic Acid, Prechorismate Pathway, Shikimate Pathway 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0415.pdf 
 Identifier    ZNC-1994-49c-0415 
 Volume    49 
67Author    Andrea Golz, HartmutK. LichtenthalerRequires cookie*
 Title    Inhibition of the Plastidic Pyruvate Dehydrogenase Complex in Isolated Plastids of Oat  
 Abstract    A cetyl-C oA Formation, A cetylm ethylphosphinate as Inhibitor, Avena sativa, de novo Fatty Acid Biosynthesis, Plastidic Pyruvate D ehydrogenase Complex (pPDHC) The activity of the plastidic pyruvate dehydrogenase complex (pPD H C) is one source of acetyl-CoA in plastids of higher plants needed for de novo fatty acid biosynthesis. This plas­ tidic enzyme reaction is specifically inhibited by acetylmethylphosphinate (AM PI), a com ­ pound which had hitherto been known only as an inhibitor of the mitochondrial pyruvate dehydrogenase complex (m PD H C). In the test system o f isolated intact oat plastids (Avena sativa) [2-14C]pyruvate was used for de novo fatty acid biosynthesis. The incorporation of label from [2-14C]pyruvate in fatty acids was inhibited by AM PI in a dose-dependent manner. The inhibition rose with increasing preincubation time of plastids with the inhibitor. I50 values for the inhibition of de novo fatty acid biosynthesis from [2-14C]pyruvate by AMPI for iso­ lated etioplasts and chloroplasts were 4.5 and 80 |i m , respectively. TTie activity of the pPDHC decreased during greening of oat seedlings, as is seen from the decreasing incorporation of [2-14C]pyruvate into fatty acids during the light-induced transformation of etioplasts into chloroplasts. In contrast to the decreasing pPDH C activity, the activity of the plastidic acetyl-C oA synthetase (ACS), which transfers acetate to acetyl-C oA, rose parallel to the transfor­ mation of etioplasts into chloroplasts. During the assay time of 20 min we could not detect an incorporation of radiolabel from pyruvate or acetate into ß-carotene or any other carotenoid. 
  Reference    Z. Naturforsch. 49c, 421 (1994); received March 25/April 25 1994 
  Published    1994 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0421.pdf 
 Identifier    ZNC-1994-49c-0421 
 Volume    49 
68Author    A. M. Akewicz, A. R. Adunz, G. H. SchmidRequires cookie*
 Title    Immunological Evidence for the Binding of ß-Carotene and Xanthophylls onto Peptides of Photosystem I from Nicotiana tabacum  
 Abstract    Photosystem I preparations were obtained from wild type tobacco Nicotiana tabacum var. John William's Broadleaf (JWB) and from the two chlorophyll-deficient mutants N tabacum Su/su and N. tabacum Su/su var. Aurea. The preparations were characterized with respect to the chlorophyll a/b ratio, their photosynthetic activity and their absorption spectroscopic properties. Peptides from these preparations were analyzed by SDS polyacrylamide gel elec­ trophoresis and transferred for the detection of bound carotenoids according to the Western blot procedure to nitrocellulose or Immobilon membranes. The PS I preparation from the wild type JW B consisted of the core and the LH CP complex. The core complex contains the two core peptides with the same apparent MW of 6 6 kD a and several peptides with the lesser molecular masses of 22, 20, 19, 17, 16, 10 and 9 kDa. The light-harvesting protein complex consists of 4 subunits with the molecular masses 28, 26, 25 and 24 kDa. The PS I preparations of the yellow-green mutant Su/su and of the A urea mutant Su/su var. Aurea contain as impurity traces of the Dl and D 2 core peptides of photosystem II and also traces of the chlorophyll-binding photosystem II peptides with the molecular masses 42 and 47 kDa. The peptides of the photosystem I preparation were characterized by specific photosys­ tem I antisera: An antiserum to the photosystem I complex reacts in the Western blot only with the homologous peptides of photosystem I. In comparative analyses with photosystem II preparations this antiserum (directed to photosystem I) reacts, as expected, only with the peptides of the light-harvesting complex. An antiserum to the C P I core peptides reacts only with the 6 6 kD a peptides of photosystem I and gives no cross reaction with heterodimer forms of the D !/D 2 core peptides of photosystem II. In the Western blot procedure by means of polyclonal monospecific antisera to carotenoids it was dem onstrated that ß-carotene is bound in high concentration onto the core peptides CPI and to a lesser extent onto the two larger subunits of the LHCP complex, exhibiting the molecular masses of 28 and 26 kDa. N eoxanthin is bound onto the same peptides. In contrast to this, lutein was only identified on the core peptides C P I and violaxanthin only on the larger subunits of the LH CP complex. As the carotenoids are labelled with antibodies, even after SDS treatm ent in the electrophoresis, it is assumed, that the carotenoids are co­ valently bound via the ionon ring to the respective peptide. 
  Reference    Z. Naturforsch. 49c, 427—438 (1994); received February 17 1994 
  Published    1994 
  Keywords    Photosystem I, ß-Carotene, Lutein, Violaxanthin, Neoxanthin, Antibodies 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0427.pdf 
 Identifier    ZNC-1994-49c-0427 
 Volume    49 
69Author    E. B. Racht, A. TrebstRequires cookie*
 Title    Hypothesis on the Control of D 1 Protein Turnover by Nuclear Coded Proteins in Chlamydomonas reinhardtii  
 Abstract    A hypothesis is presented on the events in the degradation of the D 1 protein of photosys­ tem II in the light. It proposes the existence of a nuclear encoded cleavage system that is turning over and which is m odulated by its phosphorylation state. A new experimental ap­ proach is presented in which the D 1 protein degradation under photoinhibitory light is tested in Chlam ydom onas reinhardtii grown under phosphate deficiency and pretreated with cyclo-heximide. Under these conditions the degradation of the D 1 protein is delayed whereas in C hlam y­ dom onas reinhardtii grown in full medium the D 1 protein is rapidly disappearing in high light upon addition o f chloramphenicol (CAP) or lincomycin for inhibiting the resynthesis of the D 1 protein . Cycloheximide (C H I) has little effect on photoinhibition in such control cells. In cells grown, however, for 20 h in phosphate deficiency -such that there is not yet loss of photosynthesis capacity -pretreatment with cycloheximide or canavanine in low light the degradation of the D 1 protein even in 6 h high light is prevented to an appreciable extent. Further addition of CAP or lincomycin has only a small effect. [14C]leucine incorporation was used to show that there is no resynthesis and that the presence of the D 1 protein is due to a delay of degradation. The results are interpreted to show that excess high light which converts the D 1 protein into a potentially, degradable m ode is not sufficient for degradation of the D 1 protein. A cleavage system is needed as well. It is postulated that under phosphate deficiency and pre­ treatment with CHI or canavanine a nuclear coded cleavage system for the D 1 protein is depleted, i.e. the cleavage system for the rapidly turning over D 1 is also turning over. It is shown that under phosphate deficiency an alkaline phosphatase activity in the chloro­ plast and the thylakoid membrane o f Chlam ydom onas reinhardtii is increased. It is proposed that the ratio of kinase/phosphatase converts an active, stable phosphorylated cleavage system into a labile unphosphorylated and turning over state. 
  Reference    Z. Naturforsch. 49c, 439 (1994); received January 31/May 13 1994 
  Published    1994 
  Keywords    Chlamydomonas, D 1 Protein, Photoinhibition, Photosystem II, Phosphate Deficiency 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0439.pdf 
 Identifier    ZNC-1994-49c-0439 
 Volume    49 
70Author    SabineL. Üth Jea, N. Zaléz-R, PlacidoN. Eyesb, O. Avasb, D. Laf, M. Öring3, B. Ö. Ichael, TtgRequires cookie*
 Title    Inhibition of Maize (Zea mays L.) Root Plasma Membrane-Bound Redox Activities by Coumarins  
 Abstract    Plasma Membrane, Redox Activity, Zea mays L., Dicumarol, Warfarin Modulation of plasma m embrane-bound NA DH :hexacyanoferrate III oxidoreductase activities by dicumarol and warfarin was investigated with plasma membrane vesicles of Zea m ays L. (cv. Sil Anjou 18) roots, prepared by aqueous two phase partitioning. Vesicles were about 65% right-side out orientated as dem onstrated by enzyme latency of vanadate sensitive ATPase activity. Dicumarol or warfarin, respectively, inhibited N A D H :hexacyanoferrate III oxidoreductase activity in a concentration-dependent manner and inhibition could be reversed partially by addition of quinones. 
  Reference    Z. Naturforsch. 49c, 447—452 (1994); received December 12 1993/March 8 1994 
  Published    1994 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0447.pdf 
 Identifier    ZNC-1994-49c-0447 
 Volume    49 
71Author    Y. Utaka Takeuchi, PaulJ. Birckbichler, M. Anford, K. P. Atterson, N. L. Kyung, H. Ee, En, A. C. ArterRequires cookie*
 Title    Calmodulin Regulates Nucleotide Hydrolysis Activity of Tissue Transglutaminase  
 Abstract    The interaction of calmodulin with purified guinea pig liver transglutaminase was studied. The nucleotide (ATP and GTP) hydrolysis activity of this tissue transglutaminase was tran­ siently increased and then gradually decreased depending on calmodulin concentration. The peak activation was obtained in the presence of a stoichiometric amount of calmodulin. The effect of calmodulin on the classical transglutaminase activity was minimal. Fluorescence spectroscopy dem onstrated that the enzyme produced a significant blue shift in the emission peak of dansylated calmodulin. Interestingly, Ca2+ was not required for the interaction be­ tween the two proteins. The results described here give an additional regulatory role to calmodulin. 
  Reference    Z. Naturforsch. 49c, 453—457 (1994); received March 17/May 16 1994 
  Published    1994 
  Keywords    Calmodulin, Transglutaminase, Nucleotide Hydrolysis 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0453.pdf 
 Identifier    ZNC-1994-49c-0453 
 Volume    49 
72Author    H. Einz, W. EnderothRequires cookie*
 Title    Phycoerythrin: Release from Cryptophycean Algae and Bilin Storage by the Primitive Metazoon Trichoplax adhaerens (Placozoa)  
 Abstract    Phycoerythrin, Cryptophyceae, Trichoplax, Bilin Storage Animal species that store bilins from external sources are very rare. A new example is described here. -Since the primitive marine metazoon Trichoplax adhaerens stains crimson-red when feeding on a phycoerythrin-containing alga. i.e. Pyrenomonas sp. (Cryptophyceae), the question arose whether an algal pigment can be identified as the staining matter. Thin layer chromatography and visible light absorption spectrography of aqueous Trichoplax extract disclosed several bilin components representing chromophores of phycoerythrin, a photosynthetic antenna protein that occurs only in certain algae and cyanobacteria. -Addi­ tional experiments showed that a cell-free Trichoplax extract kills and incompletely digests Pyrenom onas algae releasing phycoerythrin into the medium. These digestive faculties of Trichoplax tissue components, probably enzymes, contribute to the animal's natural feeding mechanisms that proceed extra-as well as intracorporally. While the large apoprotein compo­ nent of phycoerythrin is metabolized as a nutrient, the remaining chromophore bilins, strik­ ingly coloured tetrapyrroles, are stored within Trichoplax' distinct cellular inclusions, staining the animal crimson. 
  Reference    Z. Naturforsch. 49c, 458—463 (1994); received February 15/April 25 1994 
  Published    1994 
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 Identifier    ZNC-1994-49c-0458 
 Volume    49 
73Author    A. Kio, K. Obayashi, Shin-Ichiro, K. Ajiyam, Kunifumi Inaw, H. Iroshi, K. Anzaki, Kazuyoshi KawazuRequires cookie*
 Title    Nostodione A, a Novel Mitotic Spindle Poison* from a Blue-Green Alga Nostoc commune  
 Abstract    A novel antimitotic compound named Nostodione A (Nd A) was isolated from a terrestrial blue-green alga N ostoc commune. Nostodione A disturbed the mitotic spindle formation of sea-urchin eggs and gave small spindles with low birefringence density. Nostodione A. how­ ever. had no phytotoxicity on the germination of a dicotyledonous plant Mediccigo sativa. Based on the spectral analysis and chemical degradation, the structure of Nostodione A was elucidated. 
  Reference    Z. Naturforsch. 49c, 464—470 (1994); received February 4 1994 
  Published    1994 
  Keywords    Nostodione A, Mitotic Spindle Poison Blue-Green Alga, N ostoc commune, Sea-Urchin Eggs 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0464.pdf 
 Identifier    ZNC-1994-49c-0464 
 Volume    49 
74Author    Z. NaturforschRequires cookie*
 Title    Theoretical Studies on Molecular Determinants for Recognition at H3 Histamine Receptors  
 Abstract    A lek san d er P. M azurek and G ra żyna K arp iń ska Drug Institute,, 1994 Histamine, Methylhistamine, H3 Receptor, Molecular Orbital Calculations The determinants for recognition at H3 histamine receptors are considered. Findings based on quantum-chemical calculations suggest that H3 histamine receptor is less hydrophilic than the H2. The form most likely to be recognized by the H3 receptor is an intramolecularly hydrogen-bonded form of a-methylhistamine. Receptor environment and hydration effects of active form of histamine analogs are of crucial importance. In tro d u ctio n 
  Reference    Z. Naturforsch. 49c, 471—475 (1994); received February 17/May 5 
  Published    1994 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0471.pdf 
 Identifier    ZNC-1994-49c-0471 
 Volume    49 
75Author    G. S. Tarn Eck Er3, P.B K Och3, S. M. Atsum Otob, T. M. Itsui5, D. BiickmRequires cookie*
 Title    Localization of the Pupal Melanization Reducing Factor of Inachis io (L.) and Comparison with Melanization and Reddish Coloration Hormone  
 Abstract    In Inachis io, a pupal melanization reducing factor (PMRF) which controls morphological color adaptation is located in the brain, suboesophageal ganglion, thoracic ganglia, and all abdominal ganglia. Higher PM RF am ounts were extracted from abdominal ganglia than from the anterior ganglia. No PMRF activity could be found in the Corpora cardiaca-Corpora allata complex, in segmentally branching nerves of abdominal ganglia and their connectives. Extracts from brain-thoracic ganglia and abdominal ganglia complex of I. io contained also a factor with melanization and reddish coloration hormone (MRCH) activity in Pseudaletia separata and with pherom one biosynthesis activating neuropeptide (PBAN) activity in Bom-byx mori. However, injection of synthetic Pseudaletia pheromonotropin (Pss-PT) (= Pss-MRCH) into prepupae of I. io did not yield a melanization reducing effect. Therefore, PMRF and the PBAN/M RCH related neuropeptides seem to be different molecules. The PBAN-like factor from I. io is possibly related to the myotropins and pyrokinins of insects. 
  Reference    Z. Naturforsch. 49c, 476—482 (1994); received March 22 1994 
  Published    1994 
  Keywords    Neurohorm one, Color Adaptation, Pupal Melanization Reducing Factor, Inachis io 
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 Identifier    ZNC-1994-49c-0476 
 Volume    49 
76Author    SuzanB. Andak, M. Artin CzejkaRequires cookie*
 Title    In vitro and in vivo Binding of Epirubicin to Red Blood Cells and Human Plasma Proteins  
  Reference    Z. Naturforsch. 49c, 483 (1994) 
  Published    1994 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0483.pdf 
 Identifier    ZNC-1994-49c-0483 
 Volume    49 
77Author    Yoka Kaup3, UrsulaB. Aum Erb, Johann Kollerb, RobertE M Hedges0, H. Erbert, W. Ernerd, Hans-JürgenH. Artm, Hedwig Etspülera, Ulrich Weser3Requires cookie*
 Title    Zn2Mg Alkaline Phosphatase in an Early Ptolemeic Mummy  
 Abstract    Bone samples of a ptolem eic mummy have been employed to study the m ode of conser­ vation on the intactness of Z n2Mg alkaline phosphatase in both structure and catalytic ac­ tivity. A protein of M r = 190 ± 10 kDa being identical to the 200 kDa enzyme of fresh human bones was successfully isolated. Regardless of age 200 kDa protein bands and a distinct sub­ unit at 60 kD a were seen in SDS-PAGE electrophoresis. The 200 kDa band was also m oni­ tored by activity staining. The specific activity was 120 mU/mg and 65% of the respective activity obtained in the identical preparation using fresh human tibia or rib. The enzymic activity was inhibited in the presence of 1,10-phenanthroline and L-homoarginine. Radiocar­ bon dating supported the assignment of the mummy to the early ptolemeic period. Am ong the many bactericidal and fungicidal components employed for mummification were aro­ matic alcohols, m ono-and sesquiterpenes. Pistachio resin was the major balm resin used. The microbiological sterility o f the bone surface was ascertained by independent bacterial and fungal examinations. 
  Reference    Z. Naturforsch. 49c, 489 (1994); received March 31 1994 
  Published    1994 
  Keywords    Z n2Mg A lkaline Phosphatase, Mummified Bone, Radiocarbon Dating, Pistachio Resin, Ancient Disinfectants 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0489.pdf 
 Identifier    ZNC-1994-49c-0489 
 Volume    49 
78Author    S.Giovanni De Simoneab, J. Torres, M. Atta3, A. Nery, M. AttaaRequires cookie*
 Title    Acetylcholinesterase and Non-Specific Esterase Activities during the Regeneration of Planaria Dugesia tigrina (Girard)  
 Abstract    Biochemical modification o f the acetylcholinesterase (AChE) and non-specific esterases o f a planarian species [Dugesia tigrina (Girard)] were studied as a function o f regeneration. The enzymatic activities were measured in regenerating planarians at regular time intervals from the beginning of the regeneration process to the complete restoration of the animal. Both enzymatic activities were substantially altered during the regeneration process o f caudal and cephalic segments. Polyacrylamide gel zymograms for soluble a-naphthyl acetate hydro­ lytic activity revealed four bands of activities. These activities were fractioned into two major on cation exchange high performance h between 6 and 7 and were inhibited by PMSF, TPCK, TLCK and «-ethyl maleimide. 
  Reference    Z. Naturforsch. 49c, 501 (1994); received Decem ber 6 1993/March 8 1994 
  Published    1994 
  Keywords    Planaria, A cetylcholinesterase, Non-Specific Esterases, Regeneration 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0501.pdf 
 Identifier    ZNC-1994-49c-0501 
 Volume    49 
79Author    A. A. Nikonov, T. V. Tyazhelova, YeA. Nesterov, V. M. Rastegayeva, F. E. Ilyasov, P. V. Mashkin, B. G. KovalyovRequires cookie*
 Title    Olfactory Male Sensitivity and Its Variation in Response to Fluoranalogs of the Main Pheromone Component of Female Mamestra brassicae  
 Abstract    According to the EA G study and the field trapping tests, fluoranalogs of the main phero­ m one com ponent of Mamestra brassicae females have been found to possess disguising properties for males when used together with the main pheromone com ponent itself. In males, at low concentrations o f the above substances the diminishing of attractivity of these blends correlates with the absence of EAG responses to them. An unequal action o f these substances has been revealed in different concentration ranges of odours. The mechanisms of the action of these substances are under discussion. 
  Reference    Z. Naturforsch. 49c, 508 (1994); received September 14 1993/March 14 1994 
  Published    1994 
  Keywords    Electroantennogramme, Chemical Communication Fluoranalogs, Mamestra brassicae 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0508.pdf 
 Identifier    ZNC-1994-49c-0508 
 Volume    49 
80Author    M. Tóth, G. Szöcs, W. Francke, F. Schmidt, P. Philipp, C. Löfstedt, B. S. Hansson, A. I. FaragRequires cookie*
 Title    Pheromonal Production of and Response to Optically Active Epoxydienes in Some Geometrid Moths (Lepidoptera: Geometridae)  
  Reference    Z. Naturforsch. 49c, 516—5219 (1994); received March 9 1994 
  Published    1994 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0516.pdf 
 Identifier    ZNC-1994-49c-0516 
 Volume    49 
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