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1982 (207)
1Author    TimM. Anke, Bruno-MaxG. Iannetti, Wolfgang SteglichRequires cookie*
 Title    Antibiotika aus Basidiomyceten, XV [1]. l-Hydroxy-2-nonin-4  
 Abstract    on, ein antifungischer und cytotoxischer Metabolit aus Ischnoderma benzoinum (Wahl.) Karst. Antibiotics from Basidiomycetes. XV [1]. l-Hydroxy-2-nonyn-4-one, an Antifungal and Cytotoxic M etabolite from Ischnoderma benzoinum (W ahl.) Karst. A new antibiotic, 1-hydroxy-2-nonyn-4-one (1), has been isolated from submerged cultures of several strains of Ischnoderma benzoinum. The compound exhibits high inhibitory activity against yeasts and filamentous fungi at concentrations o f 1 -5 ng/ml. D N A , RNA, and protein syntheses in cells of the ascitic form o f Ehrlich carcinoma are strongly inhibited by the same concentrations. 
  Reference    Z. Naturforsch. 37c, 1—4 (1982); received October 31 1981 
  Published    1982 
  Keywords    Acetylenic Metabolite, Antifungal, Cytotoxic 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0001.pdf 
 Identifier    ZNC-1982-37c-0001 
 Volume    37 
2Author    Wilhelm Boland, Lothar Jaenicke, Angela BraunerRequires cookie*
 Title    Vinyl-Olefines and Sesquiterpenes in the Root-Oil of Senecio isatideus  
 Abstract    Vinyl-olefines, 1,7,10,13-Hexadecatetraene, Sesquiterpenes, Senecio isatideus (Compositae), Mass Spectroscopic Determination o f double bond positions A series of polyunsaturated vinyl-hydrocarbons («-C15 to n-C17) (10, 11, 12, 15, 16 and 17) including the as yet unknown a//-m-l,7,10,13-hexadecatetraene (15) as well as some rare sesquiterpenes such as isocomene (8) or modhephene (7) have been isolated from the root oil o f Senecio isatideus. Unambigous positioning of the double bonds o f the polyolefines was easily established by 13C-NMR spectroscopy [16]. A new mass spectroscopical method utilizing NO as a reactant gas for chemical ionization [1] made possible the reliable identification of minor and trace constituents without any chemical pretreatment or further derivatisation. 
  Reference    Z. Naturforsch. 37c, 5—9 (1982); received September 281981 
  Published    1982 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0005.pdf 
 Identifier    ZNC-1982-37c-0005 
 Volume    37 
3Author    H. Artm, K. Lichtenthaler, U. Rsula Prenzel, G.Ertrud KuhnRequires cookie*
 Title    Carotenoid Composition of Chlorophyll-Carotenoid-Proteins from Radish Chloroplasts  
  Reference    Z. Naturforsch. 37c, 10 (1982); received October 71981 
  Published    1982 
  Keywords    Raphanus sativus L, /7-Carotene, Carotenoid Composition, Chlorophyll a-Proteins, Light-Harvesting Chlorophyll, Localization of Carotenoids, Lutein, Neoxanthin 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0010.pdf 
 Identifier    ZNC-1982-37c-0010 
 Volume    37 
4Author    Hartm Ut KayserRequires cookie*
 Title    Carotenoid Biogenesis in the Stick Insect, Carausius morosus, during a Larval Instar  
 Abstract    [14C]/?-Carotene was fed to juvenile stick insects, Carausius morosus, o f the fifth instar. Radio­ activity was incorporated into 2-hydroxy-, 2-oxo-, and 3,4-didehydro-2-oxo-carotenoids o f the ß,ß-type. These transformations are due to the insect's own capacity; any contribution by microbial symbionts can be ruled out. A study on the labelling kinetics clearly shows that the biogenesis of hydroxy-and oxo-carotenoids is correlated to a decrease in the carotene precursor, but only up to mid instar. Thereafter, oxidation o f the carotene is very low but the transformations of its metabolites continue as before. Predominantly ß,^-carotene-2,2'-diol is dehydrogenated to 3,4,3',4'-tetradehydro-/?,/?-carotene-2,2'-dione via two hydroxyketones. This discontinuous utilization o f /7-carotene could be due to a stop at mid instar either in the oxidation or in the absorption in the gut o f this precursor. 
  Reference    Z. Naturforsch. 37c, 13 (1982); received September 11/October 281981 
  Published    1982 
  Keywords    Carotenoids, Metabolism, [14C]/?-Carotene, Insects, Carausius morosus 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0013.pdf 
 Identifier    ZNC-1982-37c-0013 
 Volume    37 
5Author    G. Stotz, G. ForkmRequires cookie*
 Title    Hydroxylation of the B-Ring of Flavonoids in the 3'-and 5'-Position with Enzyme Extracts from Flowers of Verbena hybrida  
 Abstract    Enzyme preparations from flowers of Verbena hybrida do not only catalyse hydroxylation of the B-ring of flavanones and dihydroflavonols in the 3'-position but also in the 5'-position. Enzyme activity for 3',5'-hydroxylation was found to be localized in the microsomal fraction and required NADPH as cofactor. Evidence is provided that the formation o f the 3',4\5'-hydroxylated flavanone (5,7,3',4',5'-pentahydroxyflavanone) and dihydroflavonol (dihydromy-ricetin), respectively, proceeds via the corresponding 3',4'-hydroxylated compounds eriodictyol and dihydroquercetin, respectively, which are most probably formed by action o f the same enzyme. Enzyme activity for 3',5'-hydroxylation was found to be strictly correlated with the prescence of 3',4',5'-hydroxylated flavonoid compounds in the flowers. 
  Reference    Z. Naturforsch. 37c, 19—23 (1982); received October 141981 
  Published    1982 
  Keywords    Anthocyanins, Flavonoids, Biosynthesis, Flavonoid 3', 5'-Hydroxylation, Verbena hybrida 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0019.pdf 
 Identifier    ZNC-1982-37c-0019 
 Volume    37 
6Author    MiguelA. De La Rosa, AntonioJ M Árquez, JoséM. VegaRequires cookie*
 Title    Dissociation of FAD from the NAD(P)H-Nitrate Reductase Complex from Ankistrodesmus braunii and Role of Flavin in Catalysis  
 Abstract    Flavin-Containing Enzyme, Nitrate Reductase, Ankistrodesmus braunii Ankistrodesmus braunii NAD(P)H-nitrate reductase is a complex hemoflavomolybdoprotein composed by eight similar subunits. The flavin prosthetic group, identified as FAD, is essential for the NAD(P)H-dependent activities of the complex, and is located before the heme chromo-phore in the enzyme electron transport chain from reduced pyridine nucleotides to nitrate. Fluorescence studies indicate that nitrate reductase can dissociate about 80% o f its FAD by incubation at room temperature, the flavin dissociation being followed by a parallel decrease of NADH-nitrate reductase activity. Dissociation o f FAD from the protein is easily increased by dilution or prolonged dialysis of the enzyme preparations. However, exogenous FAD specifically prevents the dissociation of enzyme-bound flavin, and protects the NAD(P)H-dependent activities. The K m for FAD, as a protector o f NADH-cytochrome c reductase activity, is 4 nM. In addition, dithioerythritol also prevents the flavin dissociation, and therefore the presence of free sulphydryl groups in the FAD-domain is suggested. FAD-depleted nitrate reductase, obtained by several methods, is unable to recover its original activity when incubated in the presence of FAD alone or with thiols. 
  Reference    Z. Naturforsch. 37c, 24 (1982); received July 20/0ctober 1 1981 
  Published    1982 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0024.pdf 
 Identifier    ZNC-1982-37c-0024 
 Volume    37 
7Author    HansJ. Rurainski, RichardG. Erhardt, G. Erhard, M. AderRequires cookie*
 Title    Spectrophotometric Isolation of Kinetically Different Pools of P-700 and Their Correlation to the Reduction of NADP by Isolated Chloroplasts * I. The Effect of Light Quality and Intensity  
 Abstract    Excitation of isolated chloroplasts in the presence of ferredoxin and NADP by repeated short flashes yields a polyphasic absorption change at 700 nm. Assuming first-order reactions, the signal may be resolved into three distinct components with average relaxation times o f approxi­ mately 20 (as, 150 |o.s and 20 ms. Their relative magnitude is dependent on experimental conditions; their spectral characteristics indicate that all three components may be ascribed to P-700. Concurrent measurements o f Y-NADPH, the flash yield o f N ADP reduction with an enzymatic recycling method, allowed Y-NADPH to be compared to the magnitude o f each o f the three P-700 components and to total P-700. In general, the data show a good correlation o f NADP reduction with the sum o f the ns-phases but not with the ms-phase or total P-700. Analysis of light intensity curves (blue or far red flashes) with a mathematical model which yields maximum values for all parameters at infinite light intensity shows that in both cases approximately two moles o f the microsecond component of P-700 turn over for each mole of NADPH formed. In contrast, the molar ratio of the ms-component to the yield of N ADP reduction is approx. 0.2 in blue and approx. 6.3 in far red light. The data suggest that only that portion of the P-700 pool which relaxes in the microsecond range may be involved in the reduction of N A D P while the ms-component is funtionally isolated from linear electron transport. 
  Reference    Z. Naturforsch. 37c, 31—39 (1982); received September 16 1981 
  Published    1982 
  Keywords    Flash Spectroscopy, Chloroplasts, P-700 Kinetics, N AD P Reduction 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0031.pdf 
 Identifier    ZNC-1982-37c-0031 
 Volume    37 
8Author    W. Erner, H. K. Alusa, W. Illiam, G. Filby, RuthM. ÜnznerRequires cookie*
 Title    Chemical Aspects of the Mutagenic Activity of the Ascorbic Acid Autoxidation System  
 Abstract    It has been proposed that the mutagenic activity associated with the ascorbic acid autoxidation system may involve hydrogen peroxide and peroxide radicals. We report here that the mutagenic effect may also partially reside in as yet unknown secondary products. The observed mutagenicity of 2,3-diketogulonic acid, one o f the main oxidation products, reflects its ability to form hydrogen peroxide. 
  Reference    Z. Naturforsch. 37c, 40—45 (1982); received September 16 1981 
  Published    1982 
  Keywords    Ascorbic Acid, Autoxidation, Hydrogen Peroxide, Mutagenic Effect, Oxidation Products 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0040.pdf 
 Identifier    ZNC-1982-37c-0040 
 Volume    37 
9Author    ThomasJ. Bach, H. Artm, K. LichtenthalerRequires cookie*
 Title    Mevinolin: A Highly Specific Inhibitor of Microsomal 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase of Radish Plants  
 Abstract    3-Hydroxy-3-methylglutaryl Coenzyme A Reductase, Mevalonate Formation, Mevinolin (monacolin K), Enzyme Inhibition, Biocide The fungal metabolite mevinolin, known to be a potent hypocholesterolemic agent, excerts in vitro a strong inhibitory effect on microsomal HMG-CoA reductase from etiolated radish seedlings at a concentration of about three magnitudes lower than the K m towards the natural substrate (S)-HMG-CoA (/50= 2 .5 x 10-9 m). Beside this, mevinolin significantly inhibits the root elongation of radish as well as of wheat seedlings already at low concentrations o f 10 to 100 ppb (= 2.5 x IO"8 to 2.5 x IO"7 M). 
  Reference    Z. Naturforsch. 37c, 46—50 (1982); received November 21981 
  Published    1982 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0046.pdf 
 Identifier    ZNC-1982-37c-0046 
 Volume    37 
10Author    H. Hauer, H.-D Lüdemann, R. JaenickeRequires cookie*
 Title    Free Activation Energies and Activation Volumes for the Amide Rotation in Some Peptides Studied by High Pressure 'H-High Resolution NMR  
 Abstract    From the pressure dependence o f !H high resolution N M R spectra o f two dipeptides (glycylsarcosine and N-acetyl-L-proline-NH-methylamide in the range 0.1 MPa <.p< . 150 MPa the activation volumes A V* for the am ide rotation are derived. This conform ational transition is characterized for glycylsarcosine by A V* = 4 ± 1 cm3 • m ol-1 and for. the proline derivative by AV* = 1 .5 ± 1 cm3 • m ol-1. From the given results the m axim um contribution o f proline cis ^ trans isomerisation to the pressure dependence o f the rate o f reactivation of proteins can be estimated to ~ — 30% per M Pa and proline present. 
  Reference    Z. Naturforsch. 37c, 51—56 (1982); received Septem ber 221981 
  Published    1982 
  Keywords    Activation Volume, High Pressure, NM R, Peptides, Proline-Isom erization 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0051.pdf 
 Identifier    ZNC-1982-37c-0051 
 Volume    37 
11Author    YuF. Krupyanskiib, F. Paraka, V. I. Goldanskiib, R. L. Mössbauera, E.E G Aubm Anb, H. Engelmannc, I. P. SuzdalevbRequires cookie*
 Title    Investigation of Large Intramolecular Movements within Metmyoglobin by Rayleigh Scattering of Mössbauer Radiation (RSMR)  
 Abstract    Protein Dynamic, Myoglobin, Mössbauer Effect, Rayleigh Scattering This paper reports Rayleigh scattering experiments on metm yoglobin crystals and freeze dried myoglobin which was exposed to air with different partial pressure o f water vapor. W hile dry myoglobin shows no fluctuations between conformational substates such "breathing modes" are rearly seen in water covered myoglobin. Larger amounts o f w ater increase the average mean square displacements. In crystals the dynamic behaviour is hindered by the crystal packing. The results are analysed by a theory describing the motion within the molecule by a Langevin equation with restoring forces corresponding to a square well potential. 
  Reference    Z. Naturforsch. 37c, 57—62 (1982); received Septem ber 171981 
  Published    1982 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0057.pdf 
 Identifier    ZNC-1982-37c-0057 
 Volume    37 
12Author    H. Seki, W. SchnabelRequires cookie*
 Title    On the Free Radical-Induced Aggregation of Ribonuclease — A Pulse Radiolysis Study Using the Light Scattering Detection Method  
 Abstract    The aggregation of bovine ribonuclease (RNase) induced by either -OH or BrJradicals has been studied. These radicals, which were generated by pulse radiolysis of aqueous solutions with 16 MeV electrons, readily attack the enzyme thus producing RNase-radicals which subsequently combine. At initial radical concentrations low enough (^ 0.1 radical per enzyme molecule) to prevent multimerizations other than dimerization, rate constants for the latter process were determined from the increase o f the light scattering intensity after the pulse: 2 k2 = (2.2 ± 0.3) 10® 1/mol s (Brj initiated dimerization) and (5.4 ± 0.4) 10® 1/mol s (O H initiated dimerization). The G-values for dimerization are: 1.3 (BrJ) and 0.85 (O H). Transient optical absorption measurements revealed the existence o f phenoxyl radicals of_tyrosine (TyrO-) that decayed with a rate constant o f 2 k2 (total) = (5.5 ± 0.7) 10® 1/mol s (Brj-case). The difference between k2 and k2 (total) presumably indicates the occurrence o f disproportionation. 
  Reference    Z. Naturforsch. 37c, 63—69 (1982); received September 161981 
  Published    1982 
  Keywords    Free Radical-Induced Aggregation, Ribonuclease, Light Scattering Detection Method 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0063.pdf 
 Identifier    ZNC-1982-37c-0063 
 Volume    37 
13Author    A. Ya, M. V. Potapenko, A. A. Moshnin, Krasnovsky Jr, V. L. SukhorukovRequires cookie*
 Title    Dark Oxidation of Unsaturated Lipids by the Photoxidized 8-Methoxypsoralen  
 Abstract    M ay 4/O ctober 12,1981 8-Methoxypsoralen, U ltraviolet Light, U nsaturated Lipids, Photoxidation, Chemiluminescence 8-Methoxypsoralen (8-MOP) in ethanol, acetone, benzene, or CC14 is photoxidized under UV-irradiation (320-400 nm). Photoxidized 8-MOP (0 2-8-M 0P) is stable in the organic solvents, but it is destructed in water or in liposome suspension. The destruction rate constants are 0.04 s_1 in water and 0.004 s_1 in liposom e m em branes as estim ated by the kinetics of the chemilum in­ escence accompanying the destruction. In course o f 0 2-8-M 0P destruction the residues of phospholipid unsaturated fatty acids are oxidized. G eneration of the singlet oxygen (M g) by excited 8-MOP is observed neither in acetone, nor in ethanol. Q uantum yield of M g formation in CC14 is less than 3%. A pattern is proposed for 8-M OP-sensitized oxidation of unsaturated lipids proceeding without direct attack o f lipids by singlet oxygen. 
  Reference    Z. Naturforsch. 37c, 70—7 (1982); received 
  Published    1982 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0070.pdf 
 Identifier    ZNC-1982-37c-0070 
 Volume    37 
14Author    Peter Brandt, Sabine Marten, Birgit Müller, Wolfgang WießnerRequires cookie*
 Title    Stadienspezifische Thylakoiddifferenzierung der Endocyanelle Cyanocyta korschikoffiana in der symbiontischen Assoziation mit Cyanophora paradoxa Growth Specific Thylakoid Differentiation of the Endocyanelle Cyanocyta korschikoffiana in the Symbiotic Association with Cyanophora paradoxa  
 Abstract    The thylakoid differentiation in the endosymbiotic cyanelle Cyanocyta korschikoffiana depends on the developmental stage o f the whole symbiotic association Cyanophora-Cyanocyta. D uring culturing under perm anent light the intrinsic or extrinsic location and the am ount o f the chlorophyll-protein complexes and of the phycobilines in the thylakoids change markedly. D uring this m odification o f the thylakoids the reaction centers of phytosystem I and II are more and more protected by other proteins. Moreover the am ount of phycobilisomes increases in relation to the am ount o f the chlorophyll-protein complexes. The energy transfer becomes more and more efficient. All these aspects show the typical behaviour of a mass culture of a free-living blue-green alga and imply th at Cyanocyta korschikoffiana is a symbiotic cyanelle much more than a chloroplast-like organelle. 
  Reference    Z. Naturforsch. 37c, 75—80 (1982); received October 211981 
  Published    1982 
  Keywords    Thylakoid D ifferentiation, Endocyanelles, Cyanophora paradoxa, Energy Transfer, Phycobiline 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0075.pdf 
 Identifier    ZNC-1982-37c-0075 
 Volume    37 
15Author    K. Grossmann, H. Bisswanger, H. U. SeitzRequires cookie*
 Title    Differential Fluorescence and Kinetic Studies on the Template-Binding of RNA Polymerase from Parsley and Escherichia coli  
 Abstract    A fluorescence spectroscopy m ethod is described for studying association o f RNA polymerase with DNA templates. Using double beam differential fluorescence at excitation and emission wavelengths of 285 and 335 nm, respectively, the new technique discriminates non-specific decrease of fluorescence intensity by addition o f D N A from quenching of polymerase fluorescence by protein-nucleic acid interactions. C om paring the results with studies of UM P incorporation into RNA, the Äg-values o f tem plate-binding were in good agreem ent with the values for RNA synthesis, pointing to specific interaction o f polym erase and the D NA tem plate measured by the fluorescence method. W hile E. coli enzyme showed higher affinity for tem plates such as heat-denatured poly [d(A-T)] and poly [d(G -C)] parsley RNA polym erase I accepted such templates with the same affinity as salmon sperm DNA. It is obvious that divalent cations are not necessary for the interaction of both enzymes with single-stranded DNA -tem plates. UM P incorporation studies suggest that transcription is a cooperative process. 
  Reference    Z. Naturforsch. 37c, 81—86 (1982); received O ctober 261981 
  Published    1982 
  Keywords    RNA Polymerase, Template-Binding, D ifferential Fluorescence, Parsley, E coli 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0081.pdf 
 Identifier    ZNC-1982-37c-0081 
 Volume    37 
16Author    Akira TaketoRequires cookie*
 Title    Sensitivity of Escherichia coli to Viral Nucleic Acid. XVI. Temperature Conditions for Ca2+-Dependent DNA Uptake in Escherichia coli  
 Abstract    Properties of C a2+-or Ba2+-dependent transfection and transform ation in Escherichia coli were examined, using (PX174 replicative-form (R F) D NA and plasm id DNA. F or the transfection and transformation, a heat pulse step was dispensable and the yield o f transfectants was, in most E. coli strains, rather reduced by the heat treatment. The heat pulse step was also detrim ental for the transformation o f certain strains such as lipopolysaccharide mutants. The first stage o f the DNA uptake process (formation of DNA • recipient cell complex) was dependent on low tem perature and Ca2+ ion. A substantial am ount o f the complexed R F-D N A was released from the bacteria, by washing with a chilled Tris buffer. Although a R F-D N A • cell complex was formed even at 37 °C or in chilled 0.05 m MgCl2, the complex did not yield transfectants. 
  Reference    Z. Naturforsch. 37c, 87—92 (1982); received October 141981 
  Published    1982 
  Keywords    DNA, Transfection, Transformation, Escherichia coli 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0087.pdf 
 Identifier    ZNC-1982-37c-0087 
 Volume    37 
17Author    Ryuichi Ishii, GeorgH. SchmidRequires cookie*
 Title    Studies on 180 2-Uptake in the Light by Entire Plants of Different Tobacco Mutants  
 Abstract    180 2-Uptake, Photorespiration, Tobacco M utants, Glycolate M etabolism, M ehler Reaction Photorespiratory activity was m easured in entire plants o f five tobacco variants. These tobacco variants are: the green type N. tabacum var. John W illiam 's B roadleaf (su/su Aur/aur or su/su Aur/Aur) the chlorophyll-deficient tobacco m utant Su/su (Su/su Aur/Aur) and the chlorophyll-deficient m utant Su/su var. Aurea (Su/su Aur/aur). Furtherm ore, two recently characterized phenotypes originating from N. tabacum var. Consolation namely "consolation green" (Aa Bb) and "consolation yellow-green" (aa bb). In entire plants o f these phenotypes photorespiration was measured as 180 2-uptake in the light. This uptake was com pared with the enhancem ent o f C 0 2-fixation in the W arburg effect e. when the oxygen partial pressure is lowered from 21% 0 2 to 3% 0 2. The principal conclusion from these measurem ents is firstly that under the assay conditions which are identical for all 5 phenotypes (330 ppm C 0 2, 14000 lux white light and 25 °C) all five phenotypes yield considerable differences in photorespiratory activity. Furtherm ore, we were able to show that in the different phenotypes the global 0 2-uptake in the light is repartitioned to different degrees among different m etabolic pathways. Thus, in JWB which is under the assay conditions the only fast growing species, only h alf of the m easured 180 2-uptake belongs to glycolate metabolism or photorespiration proper, the other h alf belongs to a M ehler type reaction in which excess reducing power is elim inated apparently already at the level o f photosynthetic electron transport. In the chlorophyll-deficient m utant Su/su, however, the observed 180 2-uptake in the light belongs under the assay conditions exclusively to glycolate m etabolism (no M ehler type reaction). The chlorophyll-deficient m utant Su/su var. Aurea behaves more like JWB, th at is, part of its 180 2-uptake is due to a M ehler type reaction and only the rem ainder is involved in C 0 2-metabolism, which has been already found out previously by genetic analysis. In addition photorespiration depends in Su/su more on the tem perature than in the other phenotypes tested. One of the im plications o f our results could be that it makes a difference to the plant w hether excess reducing power is disposed o f at the level o f the photosynthetic electron transport chain (via a M ehler type reaction) or at the level o f C 0 2-metabolism. 
  Reference    Z. Naturforsch. 37c, 93 (1982); received Septem ber 231981 
  Published    1982 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0093.pdf 
 Identifier    ZNC-1982-37c-0093 
 Volume    37 
18Author    T. Fujimura, I. KaetsuRequires cookie*
 Title    Immobilization of Yeast Cells by Radiation-Induced Polymerization  
 Abstract    R adiation-induced polym erization m ethod was applied to the im m obilization of yeast cells. The effects of irradiation, cooling and monom er, which are neccessary for polymerization, were recovered completely by subsequent aerobical incubation of yest cells. The ethanol productive in immobilized yeast cells increased with the increase o f aerobical incubation period. The growth of yeast cells in im m obilized yeast cells was indicated. The m axim um ethanol productivity in immobilized yeast cell system was around three times as much as that in free yeast cell system. 
  Reference    Z. Naturforsch. 37c, 102 (1982); received Septem ber 111981 
  Published    1982 
  Keywords    Yeast, Immobilization, R adiation Polymerization, R adiation Effect, Ethanol Production 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0102.pdf 
 Identifier    ZNC-1982-37c-0102 
 Volume    37 
19Author    Christian Wilhelm, Gerhard Eisenbeisb, AloysiusW. Ilda, Rudolf ZahnRequires cookie*
 Title    Nanochlorum eucaryotum: a Very Reduced Coccoid Species of Marine Chlorophyceae  
 Abstract    Nanochlorum eucaryotum was isolated from a sea water aquarium housing different sponge species, cucumarias, small crustaceans and annelids. This bright green marine alga differs from all other known coccoid species. Its most prom inent features are its very small cell size (1.5 nm) and its reduced cellular organization. Its cell contains one nucleus, one chloroplast, one mitochondrium and small vacuoles. Sometim es a Golgi apparatus can be seen. N o other subcellular features have been observed. T he cell wall is thin and smooth and does not contain any material of high electron density; only dividing cells show a rougher surface. The cells split into two daughter cells. N o sexual reproduction has been observed in this organism. We have analyzed the ultrastructural cell organization, the am ount o f total DNA and RNA per cell, the pigment composition, the growth requirem ents and the sensitivity towards different inhibitors (chloramphenicol, cycloheximid, penicillin, lysozym and cellulase). The results afford the introduction of a new species; a new family or suborder o f coccoid green algae is discussed. Diagnosis Cellula ovata et singularis, nucleo vero, mem-brana tenui et glabra aut verrucosa in casu divi-sionis. Unus chromatophorus viridi colore fulgens semperque parietalis, cellulam explens ultra dimidiam partem. Pyrenoides non observatae. Propagatio fit divisione cellulae in duas pares cellulas. Diametrus cellulae 1.5 jam (0.8-2.2 nm). The unicellular eucaryotic green alga is com­ monly surrounded by a smooth and thin cell wall. The chloroplast is bright green and parietal, oc­ cupying more than 50% of the cell. No pyrenoid is observed. In all cases only two daughter cells are formed during cell division. Dividing cells often have a rougher cell wall. The cell size varies between 0.8 nm and 2.2 pm and was found to be 1.5 pm on the average. 
  Reference    Z. Naturforsch. 37c, 107 (1982); received October 19 1981 
  Published    1982 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0107.pdf 
 Identifier    ZNC-1982-37c-0107 
 Volume    37 
20Author    Christian Wilhelm, Aloysius WildRequires cookie*
 Title    Growth and Photosynthesis of Nanochlorum eucaryotum, a New and Extremely Small Eucaryotic Green Alga  
 Abstract    Nanochlorum eucaryotum is a very small species o f unicellular coccoid green algae (1.5 nm). The growth of Nanochlorum under different conditions o f salinity, pH and light intensities was studied. Optimal growth rates were observed with normal sea water salinity and low light conditions at pH 7.0. The contents o f chlorophylls, carotinoids, soluble proteins and the chlorophyll a to chlorophyll b ratio were measured. The light saturating curves of Nanochlorum cells grown under light intensities o f 100 lx, 2000 lx and 10000 lx reveal a very narrow capacity of light adaptation. When cultured under higher light intensities, Nanochlorum was not able to reach high photosynthetic activities but underwent a photoinhibition o f photosynthesis. The contents of cytochrome f, P-700 and ribulosebisphosphate carboxylase were low and comparable with those of low light adapted Chlorella cells. The analysis o f the chlorophyll-protein complexes shows that about 80% o f total chlorophyll is bound in the light harvesting chlorophyll protein complexes. All results indicate that Nanochlorum is a low light adapted marine organism with very narrow ecological flexibility. 
  Reference    Z. Naturforsch. 37c, 115—119 (1982); received October 191981 
  Published    1982 
  Keywords    Nanochlorum eucaryotum, Growth, Photosynthesis, Cytochrome f, Chlorophyll-Protein Complexes 
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 Identifier    ZNC-1982-37c-0115 
 Volume    37 
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