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1977 (187)
1Author    H. Zehner, E. Westhof, W. Flossmann, A. MüllerRequires cookie*
 Title    Formation of H-Addition Radicals in Adenine Derivatives: Part II  
 Abstract    Electron Spin Resonance, Adenine, Radicals, INDO The formation of H-addition radicals in monocrystals of adenosine, adenosine -HC1, ade­ nine -H Cl'l H20, and adenine • 2 HC1 by X-irradiation has been studied by using electron spin resonance spectroscopy at 9.5 GHz and at 35 GHz. In all crystals, both H-addition radicals at position C2 and at position C8 were observed. The coupling constants of these two H-addition radicals are different and depend strongly on the protonation state of the adenine base. INDO cal­ culations reproduce well the observed trends of the coupling constants. It is shown that the C2-addition radical is transformed into the C8-addition radical by heat and vice versa the C8-addition into the C2-addition by light of X>360 nm. 
  Reference    (Z. Naturforsch. 32c, 1 [1977]; received October 20 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0001.pdf 
 Identifier    ZNC-1977-32c-0001 
 Volume    32 
2Author    U. F. Thomanek, F. Parak, B. WintergerstRequires cookie*
 Title    The Active Center of Methemoglobin H b (H 20 ) Investigated by Mössbauer and Susceptibility Experiments  
 Abstract    Methemoglobin, Mössbauer, Susceptibility A fast freezing technique using liquid propane was used to obtain frozen solutions of methemo­ globin at pH 7. With this method it was possible to eliminate largely the presence of a low spin component which is usually found in slowly frozen solutions but not present in the sample at room temperature. The magnetic susceptibility and Mössbauer spectra of H b(H 20) in the temperature range 4.2 K 5^ T < 250 K have been measured. The data of the high spin compound of Hb (H20) were evaluated with a Hamiltonian containing the Coulomb repulsion of the five 3d-electrons of the Fe3+ ion, a crystal electric field of C2v symmetry and the spin orbit coupling. The term describing the crystal electric field depends on five energy parameters , e2, e3, D, and E which are determined by least squares fits to the experimental data. The most relevant parameters e2 and f3 which equal the energies of the antibonding single 3d-electron orbitals 3dzJ and 3dx*_y* with respect to the 3dxy orbital are compared with earlier results of these energies e2 and s3 of the high spin compound of M b(H20). From this comparison conclusions regarding the different spatial ar­ rangements of Fe3+ in Hb(H20) and M b(H 20) are drawn. 
  Reference    (Z. Naturforsch. 32c, 11 [1977]; received November 29 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0011.pdf 
 Identifier    ZNC-1977-32c-0011 
 Volume    32 
3Author    U. P. FringeliRequires cookie*
 Title    The Structure of Lipids and Proteins Studied by Attenuated Total Reflection (ATR) Infrared Spectroscopy II. Oriented Layers of a Homologous Series: Phosphatidylethanolamine to Phosphatidylcholine  
 Abstract    Infrared Dichroism, Structure of Phospholipids, Phosphatidylcholine, Phosphatidylethanolamine Derivatives Polarized infrared ATR spectra of dry oriented multilayers of dipalmitoylphosphatidylethanol-amine, sheep brain phosphatidylethanolamine, dipalmitoylphosphatidyl-N-methylethanolamine, di-palmitoylphosphatidyl-N-N-dimethylethanolamine, dipalmitoylphosphatidylcholine and egg phos­ phatidylcholine are reported. Structural features of hydrocarbon chains and polar headgroups are discussed. The average deviation of hydrocarbon chains from the normal to the plane of the bi­ layer was found to be 20 — 30°. However it was not possible to decide whether the chains are oriented parallel to each other. The fatty acid ester groups in ß-and y-position have different conformations. The phosphate group of dipalmitoylphosphatidylethanolamine exists probably in the protonated (0 = P — OH) and not in the ionized (> P 0 2~) state. However, the latter state is ex­ pected for all other phospholipids of this series. The deviation of the bisector of <^(OPO) of the > P 0 2~ group from the normal to the bilayer is less than 45° and the mean orientation of all polar head groups is rather parallel than perpendicular to the plane of the bilayer. The polar headgroup of phosphatidylcholine assumes at least two different conformations of the O —C —C —N moiety, i. e. gauche and trans. A variety of conformers has to be expected also for the polar head groups of most of the other phospholipids investigated in this work. 
  Reference    (Z. Naturforsch. 32c, 20 [1977]; received November 15 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0020.pdf 
 Identifier    ZNC-1977-32c-0020 
 Volume    32 
4Author    W. Steglich, A. Thilmann, H. Besl, A. BresinskyRequires cookie*
 Title    2.5-Diary ley clopentan-1.3-dione aus Chamonixia caespitosa (Basidiomycetes) Pigments of Fungi, 29 1 2,5-Diarylcyclopentane-l,3-diones from Chamonixia caespitosa (Basidiomycetes)  
 Abstract    Chamonixin, 2,5-Diarylcyclopentane-l,3-diones, Fungus Pigments, Chemotaxonomy From sporophores of Chamonixia caespitosa the 2,5-diarylcyclopentane-l,3-diones gyrocyanin (1), chamonixin (2) and gyroporin (5) have been isolated, the first two being responsible for the blueing of the fruiting bodies. This result suggests a close relation of Chamonixia to the order Boletales. 
  Reference    (Z. Naturforsch. 32c, 46 [1977]; eingegangen am 22. November 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0046.pdf 
 Identifier    ZNC-1977-32c-0046 
 Volume    32 
5Author    B. V. Burger, Maritha Le Roux, C. F. Garbers, H.S C Spies, R. C. Bigalke, K.G R Pachler, P. L. Wessels, N.C R L, C.S I R, South Africa, V. Christ, K. H. MaurerRequires cookie*
 Title    Further Compounds from the Pedal Gland of the Bontebok ( Damaliscus dorcas dorcas)  
 Abstract    The identification of four further major constituents of the pedal gland exudate of the bontebok, Damaliscus dorcas dorcas, viz. a-terpineol, 2-ra-heptylpyridine, m-cresol and (Z)-6-dodecen-4-olide and the investigation of the stereochemistry of the double bond in (Z) -6-dodecen-4-olide by means of iterative computer analysis are described. An improved synthesis of this compound is outlined. Studies on Mammalian Pheromones, II The identification of 2-heptanone, 2-nonanone, 2-undecanone, 2,5-undecanedione and (Z)-5-undecen-2-one as some of the major volatile constituents of 
  Reference    (Z. Naturforsch. 32c, 49 [1977]; received July 14 1976) 
  Published    1977 
  Keywords    L Birkofer on His 65th Birthday Olfactory Communication, Pheromones, Mass Spectrometry, NMR Spectra Simulation, y-Lactone Synthesis 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0049.pdf 
 Identifier    ZNC-1977-32c-0049 
 Volume    32 
6Author    Harald RöperRequires cookie*
 Title    Analytische Untersuchungen des Wehrsekretes von Peripatopsis moseleyi (Onychophora) * Analytical Investigations of the Defensive Secretion from Peripatopsis moseleyi (Onychophora)  
 Abstract    P erip a to p sis m oseleyi, Defensive Secretion, Analysis The defensive secretion of P erip a to p sis m oseleyi (Onychophora) consists of 84% water and 16% protein and free amino acids. The secretion's defensive effectiveness is an anti-predator "sticking" action. The secretion is flung out of the oral papillae in liquid state. It is then denaturized by the air and develops increasingly sticky white threads, probably through the devel­ opment of disulfide bridges from the protein content. The elastic properties of the secretion threads indicate a micellar structure. The defensive secretion contains no volatile organic components or carbohydrates. This was confirmed by gas-liquid chromatography and thin-layer chromatography. After acidic hydrolysis of the secretion the following amino acids were determined quantita­ tively: aspartic acid, threonine, serine, proline, glutamic acid, glycine, alanine, valine, cysteine, methionine, isoleucine, leucine, tyrosine, phenylalanine, lysine, histidine and arginine. A "rare" amino acid was not identified. Tryptophane was not present (basic secretion hydrolysis). The quantita­ tive determination of free amino acids, based on the total content, showed the following results: glycine (40.9%), glutamic acid (10.8%), aspartic acid (2.65%), lysine (1.3%). Ths result shows, that the secretion is stored in a watery glycine/glutaminic acid buffer in the oral papillae of P erip a to p sis m oseleyi. High voltage paper electrophoreses and gel filtration experiments with dextran and agarose gels showed, that the secretion protein consists of, at least, two fractions with different molecular weight. 
  Reference    (Z. Naturforsch. 32c, 57 [1977]; eingegangen am 8. September 1976) 
  Published    1977 
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 Identifier    ZNC-1977-32c-0057 
 Volume    32 
7Author    Harald Röper, Kurt HeynsRequires cookie*
 Title    Spurenanalytik von /?-Benzochinon-und Hydrochinon-Derivaten mit Gaschromatographie und Gaschromatographie/Massenspektrometrie. Identifizierung von Wehrsekret-Komponenten europäischer Juliden * Trace Analysis of p-Benzoquinone-and Hydroquinone Derivatives by Gas-Liquid Chromatography and Gas-Liquid Chromatography/Mass-Spectrometry. Identification of Defensive Secretion Components from European Julids  
 Abstract    Defensive Secretions, Julida (Diplopoda) Substituted p-benzoquinones (= quinones) and substituted hydroquinones [bis-trimethylsilyl-ethers or bis-trifluoroacetates] can be separated by gas-liquid chromatography using 50 meter long thinfilm capillaries (inner diameter: 0.25 mm) coated with silicone OV 17 (50% phenyl, methyl) or silicone DC 550 (25% phenyl, m ethyl). Total retention times of various derivatives of p-benzoquinone and hydroquinone were deter­ mined. Complex model mixtures of these derivatives can be separated by gas-liquid chromatography with temperature programs and the individual components can be clearly identified by their mass spectra in the sub microgram range by using combined gas-liquid chromatography/mass-spectro-metry. This microanalytical technique was applied to identify the defensive secretion components from members of the diplopod order Julida (Arthropoda). Julus n itid u s produces a defensive secretion that consists exclusively of 2-methyl-3-methoxyquinone. The expelled defensive secretions of U nciger foetidus, C ylin droiu lu s coeru leocin ctus (londinensis), C ylin droiulu s pu n ctatu s, Cylin-droiulus luridus and O ph yiu lu s psilosu s consist of a 2-methylquinone and 2-methyl-3-methoxy-quinone mixture. The presence of the corresponding hydroquinones-2-methyl-hydroquinone and 2-methyl-3-methoxyhydroquinone-was also determined in all cases. 
  Reference    (Z. Naturforsch. 32c, 61—66 [1977]; eingegangen am 8. September/25. Oktober 1976) 
  Published    1977 
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 Identifier    ZNC-1977-32c-0061 
 Volume    32 
8Author    H. SchiechlRequires cookie*
 Title    Präparative Isolierung des Protein III der menschlichen Erythrocytenmembran Preparative Isolation of Protein III of the Human Erythrocyte Membrane  
 Abstract    Human Erythrocyte Membrane, Protein III, Isolation The paper describes a method for the large-scale isolation of protein III (protein E, major intrinsic protein) from the human erythrocyte membrane with little expenditure of time. By treat­ ment of the erythrocyte ghosts with deluted HC1 at pH 2.3 and 0 °C some membrane proteins can be extracted. From the remaining "rest"-membranes, whose major constituents, besides phos-pholipides, are protein PAS-1, other carbohydrate containing proteins and protein III, the latter can be separated in pure form by means of gel filtration. The paper reports on the amount, purity and possible structural modifications of the protein III obtained by this isolation method. 
  Reference    (Z. Naturforsch. 32c, 67 [1977]; eingegangen am 15. Oktober 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0067.pdf 
 Identifier    ZNC-1977-32c-0067 
 Volume    32 
9Author    Oskar Oster, Gerhard BuchlowRequires cookie*
 Title    Purification of Histone F3 by Covalent Chromatography  
 Abstract    The arginine-rich histone F3 has been purified by covalent affinity chromatography. By the use of activated Thiol-Sepharose 4B for the purification of cysteine containing histone F3 a highly pure protein was obtained. The simple purification procedure offers the opportunity to get larger amounts of pure histone F3 within short time. 
  Reference    (Z. Naturforsch. 32c, 72 [1977]; received October 18 1976) 
  Published    1977 
  Keywords    Histone F3, Purification, Covalent Chromatography 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0072.pdf 
 Identifier    ZNC-1977-32c-0072 
 Volume    32 
10Author    Hans-Joachim Lach, Peter BögerRequires cookie*
 Title    Isolation and Some Molecular Properties of Plastidic Algal Cytochrome b-559  
 Abstract    Cytochrome b-559, Algae, Spinach Cytochrome b-559, an integral protein of diloroplast thylakoids, was prepared in a homogeneous form from the alga B u m illeriopsis filiform is. The protein is easily denatured and can be solubilized by treatment of isolated thylakoids with high concentrations of urea and detergents in addition to weak sonification. The reduced form exhibits absorption maxima at 559, 530 and 429 nm. By comparative determination, a molecular weight of 17 000 was found for the protein from B um illeriopsis, whereas that for spinach has 37 000 daltons. Both proteins have a low, but variable lipid content which is not a necessary part of the enzymatically active cytochrome b-559. The purified cytochrome exhibits a low midpoint the preparation a transient "high-potential" form 
  Reference    (Z. Naturforsch. 32c, 75 [1977]; received November 18 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0075.pdf 
 Identifier    ZNC-1977-32c-0075 
 Volume    32 
11Author    Wolfram Trowitzsch, Hermann SahmRequires cookie*
 Title    ß -Diketoester und deren Enoläther als Aminosäure-Antagonisten On Amino Acid Antagonists: /5-Diketoesters and Their Corresponding /-Enolethers  
 Abstract    /?-Diketoesters, /?,y-Unsaturated-a-keto Acids, Amino Acid Antagonists Starting with well known /?-diketoesters the corresponding y-enolethers are synthesized and described. Both classes of compounds inhibited the growth of some microorganisms. The inhibition is abolishable by addition of certain amino acids to the definite medium. A possible mechanism of inhibition is discussed and compared with the mechanism of some /?,y-unsaturated a-amino acids. The known unsaturated a-amino acids, their origin and their biological activity are summarized in two tables. 
  Reference    (Z. Naturforsch. 32c, 78 [1977]; eingegangen am 23. August 1976) 
  Published    1977 
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 Identifier    ZNC-1977-32c-0078 
 Volume    32 
12Author    Gerhard Dietz, Christoph Woenckhaus, Rainer Jaenicke, IngeSdiuster Sandoz, Forschungsinstitut Gesellschaft, M.B HRequires cookie*
 Title    Modifizierung von Glycerinaldehyd-3-phosphat-Dehydrogenase aus Kaninchen-Skelettmuskel mit dem Coenzymanalogen [3-(3-Bromacetylpyridinio)-propyl]-adenosin-pyrophosphat Modification of Glyceraldehyde-3-phosphate Dehydrogenase from Rabbit Skeletal Muscle by [3-(3-Bromoacetylpyridinio)-propyl]-Adenosine Pyrophosphate  
 Abstract    Affinity Labeling, Glyceraldehyde-3-phosphate Dehydrogenase, Hybrid Formation The NAD analogue [3 -(3-acetylpyridinio)-propyl] adenosine pyrophosphate forms enzymically inactive complexes with glyceraldehyde-3-phosphate dehydrogenase from yeast and rabbit skeletal muscle. In the latter enzyme four mol of the analogue are bound with equal affinity inhibiting the enzyme in a competitive way: Ki = 0.3mM as compared to the dissociation constant ^ D = 0.6m M . The brominated derivative [3-(3-bromoacetylpyridinio) -propyl] adenosine pyrophosphate is co­ valently bound to both enzymes causing irreversible loss of enzymic activity. Complete inactivation of the enzyme from muscle requires two moles of the analogue per mol of tetramer. The remaining two sites are still able to bind two mol of NAD+ without regain of enzymic activity. In the case of the yeast enzyme four mol of the analogue are bound. Inactivation of the rabbit muscle enzyme is accompanied by the disappearance of two out of four highly reactive sulfhydryl groups; in the yeast enzyme the four active site cysteine residues are still able to react with DTNB, the reactivity being diminished significantly. Hybrid formation between the native enzymes from yeast and skeletal muscle is not affected by the modification of the enzyme. Similarly the sedimentation properties of the covalently modi­ fied enzyme are indistinguishable from those of the native molecule. This indicates that both the native and the irreversibly inhibited enzyme are identical regarding their quaternary structure. 
  Reference    (Z. Naturforsch. 32c, 85 [1977]; eingegangen am 7. Oktober/22. November 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0085.pdf 
 Identifier    ZNC-1977-32c-0085 
 Volume    32 
13Author    R. K. Sinha, Papiya Talapatra, Aruna Mitra, Sandip MazumdarRequires cookie*
 Title    Renaturation of Alkali-Denatured T 7 DNA Molecules Complexed with Ethidium Bromide  
 Abstract    Renaturation, DNA, Phage T7 Free and ethidium bromide (EB) complexed alkali denatured T7 DNA molecules were re-natured at 58 and 62 °C respectively for 1 -3 h. The structures of the renaturation products of the free candidates were as usual showing native like, branched and unrenatured DNA whereas the structures of the ethidium bromide complexed one were somewhat different, showing non-renatured loop-like and entangled regions present inbetween the renatured segments. On the basis of the linear base sequence of T7 DNA, these non-renatured parts are indicative of the inhibition of renaturation by the complexed EB molecules. Mapping of the non-renatured regions showed that they were present at some specific sites, which inturn suggested that the EB-binding has some base sequence specificity. 
  Reference    (Z. Naturforsch. 32c, 93 [1977]; received May 17/July 27 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0093.pdf 
 Identifier    ZNC-1977-32c-0093 
 Volume    32 
14Author    H.Wolfgang Heger, HorstW. PeterRequires cookie*
 Title    Effects of Phospholipids in the Action of Acetyl-CoA Carboxylase from Rat Liver  
 Abstract    Acetyl-CoA carboxylase (E.C. 6.4.1.2) was isolated from rat liver. The purified enzyme con­ tains phospholipids with a rather large amount of phosphatidylinositol (26%). Incubation of the purified acetyl-CoA carboxylase with phospholipase A2 (E.C. 3.1.1.4) or with phospholipase D (E.C. 3.1.1.4) diminishes the phospholipid content by 70%, this treatment leading to a complete inactivation of the enzyme. After removal of the phospholipases, the lipid-depleted enzyme can be reactivated to a certain degree by incubation with a phospholipid extract from rat liver, with phosphatidylinositol alone, or with serum albumin. 
  Reference    (Z. Naturforsch. 32c, 97 [1977]; received October 12 1976) 
  Published    1977 
  Keywords    Phospholipids, Acetyl-CoA Carboxylase, Rat Liver, Fatty Acid Synthesis, Phospholipases 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0097.pdf 
 Identifier    ZNC-1977-32c-0097 
 Volume    32 
15Author    FranzJ. Fehrenbach, H. Ansjörg EiblRequires cookie*
 Title    Interaction of Streptolysin-O with Natural and Artificial Membranes  
 Abstract    Streptolysin-O, Binding Kinetics, Biomembranes, Liposomes 1. Kinetic studies on the binding of 125I-Streptolysin-0 exhibited immediate fixation of activated toxin to natural and artificial membranes. Once fixed to the membrane no release of Streptolysin-0 or Streptolysin-O-lipid-complexes has been observed. 2. In contrast to activated toxin (free SH-groups!), oxidized Streptolysin-0 was shown to become also fixed to membranes, however, with different binding kinetics. The binding of oxidized material was clearly dependent on temperature and time. When the toxin was oxidized twice the amount of labelled material was bound as compared with the hemolytically active Streptolysin-O. This sug­ gests that oxidized Streptolysin-O, too, possesses a "binding site" within the molecule, though free SH-groups were expected to be essential for toxin fixation at the membrane. It has been shown that oxidized (inactive) and reduced (active) Streptolysin-0 forms stable "complexes" with lipo­ somes in aqueous solution, which could be separated by chromatography on Sepharose gels. 3. The binding of 125I-toxin to membranes and liposomes was specific since specific antisera against Streptolysin-0 inhibited fixation of toxin completely. 4. Hydrolysis of phospholipids and release of lysophosphatides by Streptolysin-0 esterase (EC 2.1.1.2) has not been observed, thus providing no evidence for an enzymatic concept of membrane damage. 
  Reference    (Z. Naturforsch. 32c, 101 [1977]; received September 3 1976) 
  Published    1977 
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 Identifier    ZNC-1977-32c-0101 
 Volume    32 
16Author    Ian Fry, George Papageorgiou, Elisha Tel-Or, Lester PackerRequires cookie*
 Title    Reconstitution of a System for H 2 Evolution with Chloroplasts, Ferredoxin, and Hydrogenase  
 Abstract    Continuous light-dependent H2 production was studied in a reconstituted in vitro system using S pin acea oleracea chloroplasts, C lostridiu m pasteurianum hydrogenase and S piru lin a m axim a fer­ redoxin. Photosystem Il-dependent production at 30 °C is 60 —70 /^mol H2/mg chlorophyll. At 
  Reference    (Z. Naturforsch. 32c, 110 [1977]; received December 1 1976) 
  Published    1977 
  Keywords    Biophotolysis, H2 Production, Hydrogenase, Ferredoxin, Chloroplasts 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0110.pdf 
 Identifier    ZNC-1977-32c-0110 
 Volume    32 
17Author    GeorgH. Schmid, Helga List, Alfons RadunzRequires cookie*
 Title    Inhibition of Photosystem II-Reactions in Blue-Green Algae by the Antisera to Lutein and Neoxanthin  
 Abstract    Thylakoid Membrane, Photosystem-II, Carotenoids, Antiserum An antiserum to lutein agglutinates thylakoids of N ostoc m uscorum and O scillatoria chalybea. From this it follows that lutein is located in the outer surface of the thylakoid membrane of these blue-green algae. The same result is obtained for an antiserum to neoxanthin. As neoxanthin is supposed not to occur in blue-green algae it follows that in this case the antibody action should be directed towards a carotenoid with allenic structure. The antisera to lutein and neoxanthin inhibit in both investigated algal species photosynthetic electron transport on the oxygen-evolving side of photosystem II. Moreover, the inhibition sites of both antisera are identical in N ostoc m uscorum and are located between the sites of electron donation of the artificial electron donors tetramethyl benzidene and diphenylcarbazide. In the case of the blue-green alga O scillatoria chalybea the inhibition sites of both antisera differ. Whereas the inhibition site of the antiserum to neoxanthin lies again between the sites of electron donation of tetramethyl benzidine and di­ phenylcarbazide, the inhibition site of the antiserum to lutein appears to be situated at least partially beyond the site of electron donation of tetramethyl benzidine. The degree of inhibition of electron transport reactions with N ostoc m uscorum is for both antisera 50 — 60 per cent and is pH-dependent. The pH-optimum lies at pH 7.2 for the antiserum to neoxanthin and at 7.8 for the antiserum to lutein. In comparison to this data the same antisera inhibit electron transport in chloroplasts from higher plants only by 20%. This low degree of inhibition in higher plants is apparently due to the fact that the surfaces of the thylakoids are not accessible to antibodies within the grana. In contrast to this the thylakoid surfaces of blue-green algae are fully accessible because the thylakoids are unstacked. The thylakoids of O scillatoria chalybea have the tendency towards aggregation. Therefore, the results concerning the accessibility of the carotenoids to antibodies are not so clear cut as with N o sto c m uscorum . 
  Reference    (Z. Naturforsch. 32c, 118 [1977]; received October 18 1976) 
  Published    1977 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0118.pdf 
 Identifier    ZNC-1977-32c-0118 
 Volume    32 
18Author    K. Arl, Georg Götz, Simon GötzRequires cookie*
 Title    Normale Entwicklung der Fliege Drosophila in Niederfrequenten Magnetfeldern Normal Development of the Fruitfly D rosophila in VLF Magnetic Fields  
 Abstract    Attempts to substantiate irreversible actions of a variety of magnetic fields on the fruitfly, D rosophila m elanogaster, have been successful and unsuccessful in about equal numbers. The most conspicuous mutagenic effects apparently induced by pulsed H F-fields1 failed to appear under continuous electromagnetic irradiation 2. This seems to correlate the observed damage with the VLF-components of the pulsed fields. The present investigation is motivated by the occurrence of these components both in the atmosphere and in the vicinity of electrical appliances. A strain of nor­ mally viable wild type males and subnormally viable A ttach ed-X y w females was used in which the yield, and the sex ratio, of the progeny indicate, respectively, the extent of developmental damage and of sex-linked recessive lethal mutation induced by the exposure to detrimental con­ ditions. Evaluation of 73,800 flies from subsequent generations of a control group and two test groups raised in steady, or rotating, homogeneous 9.6 kHz magnetic fields of about 2.5 G did not 
  Reference    (Z. Naturforsch. 32c, 125 [1977]; eingegangen am 2. September 1976) 
  Published    1977 
  Keywords    Electromagnetic Fields, Biomagnetism, Morphogenesis, Gene Mutation, Fruitfly D rosophila 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0125.pdf 
 Identifier    ZNC-1977-32c-0125 
 Volume    32 
19Author    D. W. Liibbers, N. Opitz, P. P. Speiser, H. J. BissonRequires cookie*
 Title    N anoencapsulated * Fluorescence Indicator M olecules M easuring pH and p 0 2 D ow n to Subm icroscopical R egions on the Basis of the O ptode-Principle *  
 Abstract    To measure p 0 2 in gases or fluids and pH in solutions the fluorescence indicators pyrene butyric acid and ß-m e-thylumbelliferone, respectively, were nanoencapsulated to obtain nano-probes for measurement in physiological struc­ tures of nano-range. For pH the fluorescence changes of /?-methylumbelliferone were monitored, for p0 2 the fluo­ 
  Reference    (Z. Naturforsch. 32c, 133 [1977]; received October 18 1976) 
  Published    1977 
  Keywords    Fluorescence Photometry, Oxygen Pressure, Hydrogen Activity, Nanoencapsulation, Fluorescence Indicators 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0133_n.pdf 
 Identifier    ZNC-1977-32c-0133_n 
 Volume    32 
20Author    J.G R ElferinkRequires cookie*
 Title    F luorescence and M embrane-Action of Tetracaine  
 Abstract    Tetracaine, Fluorescence, Erythrocyte Membrane The fluorescence of tetracaine depends on the micro­ environment of the molecule and increases with increasing hydrophobicity. The presence of erythrocyte membranes strongly enhances tetracaine fluorescence. The results sup­ port the view that the alkyl chain and aromatic part of tetra­ caine is embedded in apolar regions of the lipid or protein phase of the membrane. 
  Reference    (Z. Naturforsch. 32c, 135 [1977]; received November 29 1976) 
  Published    1977 
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 Identifier    ZNC-1977-32c-0135_n 
 Volume    32 
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