| | 2 | Author
| Richard Wahl, Ekkehard Kallee | Requires 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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| default:Reihe_C/29/ZNC-1974-29c-0608.pdf | | | | Identifier
| ZNC-1974-29c-0608 | | | | Volume
| 29 | |
| 3 | Author
| Edward Göbel, Ruth Riessner, Peter Pohl | Requires 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 | |
| 4 | Author
| Jiro Hoshino, Uta Kühne, Branka Filjak, Hans Kröger | Requires 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 | |
| 6 | Author
| Paul Hansmann, Peter Sitte | Requires 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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| default:Reihe_C/39/ZNC-1984-39c-0758.pdf | | | | Identifier
| ZNC-1984-39c-0758 | | | | Volume
| 39 | |
| 8 | Author
| MatildeBarón Ayala, Gerhard Sandmann | Requires 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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| default:Reihe_C/43/ZNC-1988-43c-0438.pdf | | | | Identifier
| ZNC-1988-43c-0438 | | | | Volume
| 43 | |
| 9 | Author
| JaspreetA. Rora, P. V. Sane | Requires 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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| default:Reihe_C/44/ZNC-1989-44c-0537.pdf | | | | Identifier
| ZNC-1989-44c-0537 | | | | Volume
| 44 | |
| 10 | Author
| J. Arora, P. Nath, P. V. Sane | Requires 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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| default:Reihe_C/48/ZNC-1993-48c-0795.pdf | | | | Identifier
| ZNC-1993-48c-0795 | | | | Volume
| 48 | |
| 12 | Author
| KarlSiegfried Boos, Eckhard Schlimme, Paderborn, Morio Ikehara | Requires 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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| default:Reihe_C/33/ZNC-1978-33c-0552.pdf | | | | Identifier
| ZNC-1978-33c-0552 | | | | Volume
| 33 | |
| 14 | Author
| G. Ünter Müller, W. Olfhard Bandlow | Requires 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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| default:Reihe_C/42/ZNC-1987-42c-1291.pdf | | | | Identifier
| ZNC-1987-42c-1291 | | | | Volume
| 42 | |
| 15 | Author
| J. Schole, Chr Schole, J. Eikemeyer | Requires 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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| default:Reihe_C/49/ZNC-1994-49c-0657.pdf | | | | Identifier
| ZNC-1994-49c-0657 | | | | Volume
| 49 | |
| 16 | Author
| Andrzej Szczepaniak3, Karin Frankb, Jacek Rybkaa | Requires 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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| default:Reihe_C/50/ZNC-1995-50c-0535.pdf | | | | Identifier
| ZNC-1995-50c-0535 | | | | Volume
| 50 | |
| 17 | Author
| Coralie Wink, Thom As, H. Artm Ann | Requires 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 | |
|
