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1Author    W. Schreibmayer, H. Hagauer, H. A. TritthartRequires cookie*
 Title    Incorporation of a Voltage Sensitive Pore from Guinea Pig Heart Mitochondria into Black Lipid Membranes and Characterization of Electrical Properties  
 Abstract    A pore from guinea pig heart mitochondria has been incorporated into BLM 's (Black lipid membranes) in a highly oriented manner and its electrical properties studied. The pore shows multistate behaviour, the distribution of the pore between different conducting states being very sensitive to voltage. This has been proven by computation of single-pore experiments. Highest single pore conductance was 4.5 nSi in 1 M KC1, independent of voltage and with no detectable preference for cations or anions. The pore from guinea pig heart mitochondria reacts more sensitivly to voltage than pores of mitochondria from other tissues so far incorporated into BLM's. 
  Reference    Z. Naturforsch. 38c, 664—667 (1983); received February 23 1983 
  Published    1983 
  Keywords    Pore, Mitochondria, Reconstitution Black Lipid Membranes 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0664.pdf 
 Identifier    ZNC-1983-38c-0664 
 Volume    38 
2Author    Richard Wahl, Ekkehard KalleeRequires cookie*
 Title    Einfluß verschiedener Medikamente auf die Bindung von Schilddrüsenhormonen an Lebermitochondrien Influence of Various Drugs on the Adsorption of Thyroid Hormones to Liver Mitochondria  
 Abstract    Distribution 1. [131I] L-thyroxine (T4) or [131I]L-triiodothyronine (T3) was added in 50 pM — 25 nM and 26 pM —132 nM concentrations to suspensions of rat liver mitochondria. In distribution equilibria between soluble proteins and mitochondria the adsorption of the thyroid hormones to the mito­ chondria followed an approximately linear function when the radioactive hormones were added within the range of physiological concentrations. At identical protein concentrations T3 was ad­ sorbed to the mitochondria one tenth more strongly than T4 when neither serum proteins nor cell sap had been added. The adsorption of both T3 and T4 to mitochondria and soluble proteins is reversible. The distribution of the thyroid hormones between organelles and soluble proteins depends on the ratio of the protein concentration in the sedimented mitochondria to the protein concentration in the supernate after centrifugation. The desorption of T3 and T4 from the mito­ chondria by soluble proteins, however, represents no linear function. 2. The distribution equilibria of simultaneously added 131I —T4 and 125I —T3 can be shifted by certain drugs. Chlorpromazin and dinitrophenol displaced the thyroid hormones from their binding to soluble proteins onto the mitochondria. Vice versa, phenylbutazone, phenytoin, brom-sulfalein and silymarin displaced the hormones from the mitochondria more strongly than from soluble proteins. Sodium oleate displaced the hormones in both directions. Minor shifting effects or none at all could be detected when several other drugs were used. The described procedure apparently yields new information on some effects of drug action. 
  Reference    (Z. Naturforsch. 29c, 608 [1974]; eingegangen am 14. Mai 1974) 
  Published    1974 
  Keywords    Equilibria, Drug Action, Mitochondria, Protein Binding, Thyroid Hormones 
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 TEI-XML for    default:Reihe_C/29/ZNC-1974-29c-0608.pdf 
 Identifier    ZNC-1974-29c-0608 
 Volume    29 
3Author    Edward Göbel, Ruth Riessner, Peter PohlRequires cookie*
 Title    Einfluß von DCMU auf die Bildung von Lipiden und Fettsäuren und auf die Ultrastruktur von Euglena gracilis Influence of DCMU on the Formation of Lipids and Fatty Acids, and on the Ultrastructure of Euglena gracilis  
 Abstract    Euglena g racilis Klebs (strain Z) was grown heterotrophically in the dark for 6 days. Sub­ sequently, the cells were grown photoautotrophically under white fluorescent light with varying amounts of 3-(3,4-dichlorophenyl)-l,ldimethyl urea (DCMU) (1 .7 X 1 0 -9 — 1 .0 X 1 0 -5 mol/1) added 
  Reference    (Z. Naturforsch. 31c, 687 [1976]; eingegangen am 9. März/20. September 1976) 
  Published    1976 
  Keywords    Euglena gracilis, Fatty Acids, Lipids, Ultrastructure, Chloroplasts, Mitochondria 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0687.pdf 
 Identifier    ZNC-1976-31c-0687 
 Volume    31 
4Author    Jiro Hoshino, Uta Kühne, Branka Filjak, Hans KrögerRequires cookie*
 Title    Regulation and Characterization of L-Serine: Pyruvate Aminotransferase in Rat Liver Cytosol and Mitochondria  
 Abstract    Distribution of rat liver serine: pyruvate aminotransferase between cytosol and mitochondria varies considerably with the dietary and hormonal state of animals. Feeding a high-protein diet or fasting the animals results in an increase in the enzyme activity of both fractions but more marked in the mitochondrial fraction. A low-protein diet exerts the reverse effect. A single ad­ ministration of dibutyryl cyclic AMP causes a rapid elevation of the enzyme activity in both fractions, which is effectively prevented by cycloheximide, actinomycin D and cortisone. The activity in mitochondria increases with a lag of 2 h following injection of the nucleotide inducer, in contrast to the cytosol enzyme, which increases without any lag. Gel filtration and DEAE cellulose chromatography of the enzyme from both fractions revealed the similar pattern and some kinetic constants of these two types of the enzyme were not significantly different from each other. These results indicate that rat liver serine: pyruvate aminotransferase is synthesized in the extra-mito-chondrial site and transfered to mitochondria. 
  Reference    (Z. Naturforsch. 32c, 249 [1977]; received January 13/February 21 1977) 
  Published    1977 
  Keywords    Serine: Pyruvate Aminotransferase, Cytosol, Mitochondria, Dibutyryl Cyclic Adenosine Monophosphate 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0249.pdf 
 Identifier    ZNC-1977-32c-0249 
 Volume    32 
5Author    K. T. RindierRequires cookie*
 Title    Die Temperaturabhängigkeit biologischer Prozesse Temperature-Dependence of Biological Process  
 Abstract    Temperature dependence of biological processes is described by the modified Arrhenius equa­ tion, in which the constant is replaced by a temperature-variable coefficient. The theoretical foun­ dation for this replacement is given and experimentally verified. 1. Die Tem peraturabhängigkeit der Geschwindig­ keit chemischer Reaktionen wird durch die A rrhe­ niusgleichung beschrieben: v = v0 -e~ ElR T . 
  Reference    Z. Naturforsch. 34c, 474 (1979); eingegangen am 11. April 1978 
  Published    1979 
  Keywords    Arrhenius Equation, Phase-Change, Water, Mitochondria, Metabolizing Cell 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0474.pdf 
 Identifier    ZNC-1979-34c-0474 
 Volume    34 
6Author    Paul Hansmann, Peter SitteRequires cookie*
 Title    Comparison of the Polypeptide Complement of Different Plastid Types and Mitochondria of Narcissus pseudonarcissus  
 Abstract    The protein complement of chloroplasts, prochromoplasts, chromoplasts, and mitochondria of the daffodil (Narcissus pseudonarcissus) has been investigated comparatively by gel electro­ phoresis. Mitochondria do not share common proteins with plastids. On the other hand, there is a broad overlap of the protein complement of the three plastid types investigated, in spite of their different fine structures. There are, however, remarkable differences regarding the relative amounts of many protein species, and certain plastid proteins are entirely absent either from the chloroplasts (e.g., 2 chromoplast proteins in the 60 kDa range) or the chromoplasts (e.g., LHCP). The protein complement of prochromoplasts, which contain chlorophylls and the LHCP, is nevertheless quite more similar to the protein pattern of the chromoplasts than to the one of the chloroplasts. 
  Reference    Z. Naturforsch. 39c, 758—766 (1984); received May 9 1984 
  Published    1984 
  Keywords    Narcissus, Plastids, Mitochondria, Protein Complement, SDS-PAGE 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0758.pdf 
 Identifier    ZNC-1984-39c-0758 
 Volume    39 
7Author    Rüdiger Riehl, Volker WalldorfRequires cookie*
 Title    Raillietiella aegypti (Pentastomida, Cephalobaenida)  
 Abstract    The oocytes of the cephalobaenid Pentastomid Rail­ lietiella aegypti were studied by electron microscopy. A prominent feature of vitellogenic oocytes are numerous spherical, oval and elongated mitochondria. Some of these are shown with desmosome-like structures. The associa­ tions between mitochondria and the desmosome-like struc­ tures have always been observed to lie freely in the oocyto-plasm; there are no apparent connections with the oocytous plasma membrane. Possible functional roles of these com­ plexes are evaluated. 
  Reference    Z. Naturforsch. 40c, 748—750 (1985); received July 10 1985 
  Published    1985 
  Keywords    Oocytes, Mitochondria, Desmosome-like Structure, Rail­ lietiella aegypti, Pentastomida 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0748_n.pdf 
 Identifier    ZNC-1985-40c-0748_n 
 Volume    40 
8Author    MatildeBarón Ayala, Gerhard SandmannRequires cookie*
 Title    The Role of Cu in Respiration of Pea Plants and Heterotrophically Growing Scenedesmus Cells  
 Abstract    In Scenedesmus about half of NADH oxidation proceeds via a cyanide-sensitive and the other half via a cyanide-insensitive respiratory pathway. In contrast, respiration is completely cyanide sensitive in pea indicating that the alternative respiratory pathway is absent. Cu deficiency in pea plants and in heterotrophically grown Scenedesmus cells interferes with respiratory activity of mitochondria. In both organisms, the cyanide-sensitive NADH oxidation was strongly decreased during cultivation in low Cu media. Cu sensitivity was also observed for the alternative respiratory pathway in Scenedesmus. These results suggest that a Cu-containing component is involved in the alternative respiratory pathway. This is the main reason why alternative respiration cannot be regarded as a compensation for low cytochrome-oxidase activities during Cu starvation. The Cu dependency of the cyanide-sensitive respiration was located at the site of cytochrome oxidase. A strong coordination of the biosynthesis of the Cu-containing cytochrome-oxidase complex was evident. When the endogenous Cu pool was low, formation of cytochrome aa 3 , another component of cytochrome oxidase, was also decreased. 
  Reference    Z. Naturforsch. 43c, 438—442 (1988); received December 7 1987/February 10 1988 
  Published    1988 
  Keywords    Cu Deficiency, Cytochrome Oxidase, Mitochondria, Pea Plants, Scenedesmus 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0438.pdf 
 Identifier    ZNC-1988-43c-0438 
 Volume    43 
9Author    JaspreetA. Rora, P. V. SaneRequires cookie*
 Title    Histidyl Residues Mediate Electron Transport in Plant Mitochondria  
 Abstract    Plant The effect of chemical modification of histidyl residues using diethyl pyrocarbonate (D EP) on plant mitochondrial electron transport was studied. Mitochondrial membranes from potato tubers were isolated and electron flow from N A D H to oxygen, NADH to ferricyanide and ascorbate to oxygen were monitored in pro», nee and/or absence of DEP. Measurements were made at various concentrations of DEP and at different pHs either by using an oxygen electrode or spectro-photometrically. The results show that DEP inhibits flow of electrons from NADH to oxygen, however partial electron transport from N A D H to ferricyanide and ascorbate to oxygen was unaffected. Maximum inhibition was observed at pH 6.5. The time course of the DEP action revealed a biphasic nature of inhibition. Effects on the levels of reduction of cytochromes b and c by DEP during electron transport indicated that histidyl residues may be present before or at cytochrome b , which are being modified. 
  Reference    Z. Naturforsch. 44c, 537 (1989); received April 7 1989 D edicated to 
  Published    1989 
  Keywords    Mitochondria, Histidine Modification, Electron Transport, Spectral Studies 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0537.pdf 
 Identifier    ZNC-1989-44c-0537 
 Volume    44 
10Author    J. Arora, P. Nath, P. V. SaneRequires cookie*
 Title    Translocation of Adenine Nucleotides in the Mitochondria of Male Sterile and Male Fertile Sorghum  
 Abstract    The translocation of ATP from the inside to the outside of the mitochondrial membrane has been studied in a male sterile (2219 A) and a male fertile (2219 B) line of sorghum. The translocation of ATP was found to be substantially lower in case of mitochondria from the male sterile line. The affinity of adenine nucleotides to the translocator proteins of the mito­ chondrial membrane was found to be almost one half in case of 2219 A as compared to 2219 B when the K m for ATP-ADP was determined by two different assays. It is proposed that the inadequate supply of ATP in the cytosol resulting from its inefficient translocation may con­ tribute to the male sterility in this line. 
  Reference    Z. Naturforsch. 48c, 795—798 (1993); received May 14/ 
  Published    1993 
  Keywords    ATP-ADP Translocation, Cytoplasmic Male Sterility, Sorghum, Mitochondria 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0795.pdf 
 Identifier    ZNC-1993-48c-0795 
 Volume    48 
11Author    W. Müller-Klieser, W. KreutzRequires cookie*
 Title    O n the Cross-Section Structure of the Mitochondrial Cristae-Membrane as Revealed by X-Ray Diffraction  
 Abstract    Mitochondria were isolated using sorbitol and high buffer concentration in the medium. X-ray diffraction patterns arising from the mitochondrial cristae-membrane were recorded in the fully dried state and in two different states in humidity. The (Munction evaluation of these X-ray dif­ fraction diagrams resulted in electron density cross-section profiles, which consist of two main peaks of opposite sign and one, respectively two, brane amounts to 120 Ä in the dry and 140 Ä to cross-section profile is tentatively proposed. 
  Reference    (Z. Naturforsch. 31c, 612 [1976]; received July 16 1976) 
  Published    1976 
  Keywords    Biomembranes, Mitochondria, X-Ray Diffraction, (^-Function, Electron Density Profile 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0612.pdf 
 Identifier    ZNC-1976-31c-0612 
 Volume    31 
12Author    KarlSiegfried Boos, Eckhard Schlimme, Paderborn, Morio IkeharaRequires cookie*
 Title    Conformationally Restricted Adenine Nucleotide Analogs in Mitochondrial Adenine Nucleotide Transport  
 Abstract    The conform ationally restricted adenine nucleotide analogs 8,3'anhydro-8-oxy-9-(/?-D-xylofurano-syl) adenine-5'-0-tri (d i) -phosphate (I) , and 8,2'-anhydro-8-oxy-9-(/5-D-arabinofuranosyl) adenine-5'-0-tri (di)-phosphate (II), were prepared chemically as their a-32P-labelled compounds and compared with syn-structured 8-bromo A T (D) P in mitochondrial adenine nucleotide translocation. The experimental findings demonstrate that the heterocycle-ribose orientation affects the carrier mediated adenine nucleotide transport very strongly, anti region is prerequisite for the bound nucleotide nucleotide carrier. 
  Reference    Z. Naturforsch. 33c, 552 (1978); received March 23/May 3 1978 
  Published    1978 
  Keywords    Conform ationally Restricted Adenine Nucleotides, Mitochondria, Adenine Nuclcotide Carrier, Translocation, Transport 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0552.pdf 
 Identifier    ZNC-1978-33c-0552 
 Volume    33 
13Author    AnaR. De Boland, RicardoL. BolandRequires cookie*
 Title    Effects o f Vitamin D 3 on in vivo Labelling o f Chick Skeletal M uscle Proteins with pHJLeucine  
 Abstract    The effects o f the administration o f a single oral dose o f vitamin D 3 to rachitic chicks on the in vivo incorporation o f [3H]leucine to proteins o f skeletal muscle subcellular fractions was studied. A significant stim ulation (50%) o f labelling o f mitochondrial proteins could be seen. The sterol affected the labelling o f sarcoplasmic reticulum (20%) and contractile proteins (10%) to a lesser extent. These results confirm previous observations which im ­ plicate vitamin D 3 in the synthesis o f m itochondrial proteins. 
  Reference    Z. Naturforsch. 39c, 1015—1016 (1984); received April 24 1984 
  Published    1984 
  Keywords    Skeletal Muscle, Mitochondria, [3H]Leucine Labelling, Rickets, Vitamin D 3 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1015_n.pdf 
 Identifier    ZNC-1984-39c-1015_n 
 Volume    39 
14Author    G. Ünter Müller, W. Olfhard BandlowRequires cookie*
 Title    cA M P-Dependent Protein Kinase Activity in Yeast Mitochondria  
 Abstract    Two different cAMP-binding proteins have been identified in yeast mitochondria by photo­ affinity labelling and based on the occurrence of cAMP-binding activity in two different sub-mito­ chondrial fractions. One protein (M r 45—46000) is tightly bound to the inner mitochondrial membrane whereas the other (M r 42000) is found in the soluble intermembrane space. With endogenous substrate cAMP-dependent protein kinase activity could not be demonstrated with sufficient clarity. However, using acidic heterologous substrates, like casein and phosvitin, one cAMP-dependent protein kinase was identified in the intermembrane space. Only low phosphate incorporation was found using histone fractions as substrate. cAMP-dependent modification of proteins appears to be very shortlived in mitochondria. Its physiological significance remains unknown, since neither mitochondrial transcription, translation, respiration nor import of cyto-plasmically synthesized precursors into mitochondria appear to be influenced by exogenous cAMP either in vivo or in vitro. It is shown that cAMP is not actively transported into the inner mitochondrial compartment but rather binds to a receptor(s) localized outside the permeability barrier provided by the inner membrane. 
  Reference    Z. Naturforsch. 42c, 1291 (1987); received May 29/August 3. 1987 
  Published    1987 
  Keywords    cAMP-Dependent Protein Kinase, Protein Phosphatase, Yeast, Mitochondria, Sub-Mitochon-drial Location 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-1291.pdf 
 Identifier    ZNC-1987-42c-1291 
 Volume    42 
15Author    J. Schole, Chr Schole, J. EikemeyerRequires cookie*
 Title    Diethyl Phosphate Binding to Mitochondrial Cardiolipin after Intraportal Infusion in Rats  
 Abstract    20 min after intraportal infusion of diethyl phosphate (DEP) in rats, the mitochondrial cardiolipin (CL; 1,3-bisphosphatidyl glycerol) fraction is labelled with DEP. The obtained mixture of CL and DEP-labelled CL, which up to now has not been separated, behaves chromatographically (fractogel; HPLC; TLC), in respect to release of DEP and also in respect of the 31P NMR spectrum as a mixture of CL and cardiolipin ketone diethylenol phosphate. The latter compound was also obtained by photochemical reaction of CL ketone with diethyl phosphoric acid. After cautious hydrogenation (palladium charcoal) of the total mitochondrial lipid fraction of rats treated with DEP and subsequent extraction with NaCl solution (0.005 mol/1), glycerol-2-DEP has been identified in the water phase. It is supposed that this phosphoric acid derivative is formed from CL-DEP by elimination of two molecules of phosphatidic acid. 
  Reference    Z. Naturforsch. 49c, 657—664 (1994); received May 16/ July 6 1994 
  Published    1994 
  Keywords    Mitochondria, Cardiolipin, Cardiolipin Ketone, High-Energy Phosphate, Diethyl Phosphate 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0657.pdf 
 Identifier    ZNC-1994-49c-0657 
 Volume    49 
16Author    Andrzej Szczepaniak3, Karin Frankb, Jacek RybkaaRequires cookie*
 Title    Membrane Association of the Rieske Iron-Sulfur Protein  
 Abstract    The mode of membrane attachm ent of the Rieske iro n -su lfu r proteins from cytochrome b(,f complex of pea thylakoids and from cytochrome bcx complex of yeast mitochondria has been studied using biochemical approaches. The relative sensitivity of the Rieske protein to trypsin in the thylakoid membrane shows that all trypsin sites of the Rieske protein are on the lumen side of the thylakoid membrane. In contrast to cytochrome / the chloroplast Rieske protein was extracted from thylakoids using chaotropic agents (NaSCN, urea), an alkaline pH and relatively low concentrations of Trinon X-100. The cytochrome bcx complex Rieske protein from mitochondrial membranes of yeast was also released by NaSCN and alkaline treatm ent. The results presented here led us to the conclusion, that the mitochondrial and chloroplast Rieske proteins are extrinsic and that their association with the rest of the complex involves hydrophobic interactions. 
  Reference    Z. Naturforsch. 50c, 535—542 (1995); received January 1/February 27 1995 
  Published    1995 
  Keywords    Chloroplast, Mitochondria, Cytochrome b6f Complex, Cytochrome bcx Complex, Rieske Protein 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0535.pdf 
 Identifier    ZNC-1995-50c-0535 
 Volume    50 
17Author    Coralie Wink, Thom As, H. Artm AnnRequires cookie*
 Title    Properties and Subcellular Localization of L-Alanine: Aldehyde Aminotransferase: Concept of an Ubiquitous Plant Enzyme Involved in Secondary Metabolism  
 Abstract    L-Alanine: aldehyde aminotransferase occurs ubiquitously in higher plants. The enzyme catalyzes the reaction: L-alanine + monoaldehyde -> monoamine + pyruvate; it is responsible for the formation of aliphatic plant amines and involved in the biosynthesis o f hemlock alkaloids as shown by Roberts. A continuous coupled photometric test was developed to determine the low activities of the transaminase. The enzyme from the "amine-free" plant Spinacia oleracea was purified 77-fold and separated from other aminotransferases. A comparison of the Spinacia enzyme with that isolated from spadix-appendices o f the amine-producing Arum maculatum during anthesis revealed very similar characteristics in pH-dependence, ATm-values for alanine and aliphatic aldehydes, and inhibition by 2-oxoacids. In contrast to the Spinacia enzyme the Arum aminotransferase is rapidly inactivated in the absence o f pyridoxal-5'-phosphate. The enzymes o f S. oleracea, A. maculatum and Mercurialis perennis are localized in mitochondria, but not in chloroplasts or peroxisomes. The results are discussed in relation to the function o f alanine: aldehyde aminotransferase in secondary metabolism. It is suggested that some enzymes may be expressed in plants at low levels, even in the absence o f any metabolic function. 
  Reference    Z. Naturforsch. 36c, 625 (1981); received April 13 1981 
  Published    1981 
  Keywords    Spinacia oleracea, Arum maculatum, Alanine: Aldehyde Aminotransferase, Amine-Biosynthesis, Subcellular Localization, Mitochondria 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0625.pdf 
 Identifier    ZNC-1981-36c-0625 
 Volume    36