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1Author    Hartmut Holz, Lerke ScholingRequires cookie*
 Title    Charakterisierung von Messenger-Ribonukleoproteiden aus Hefezellen Characterization of Messenger Ribonucleoproteins from Yeasts  
 Abstract    A method to produce in 15 min stable sphaeroplasts from yeasts of the early log-phase is de­ scribed. This method was used to isolate polysomes, after specific radioactive labelling of mRNA. The mRNP *-particles, isolated from polysomes, have sedimentation-coefficients from 10 to 80S and a density of 1.4 g/cm3, the polysomes a density of 1.58 g/cm 3 and the ribosomes a density of 1.61 g/cm3. 
  Reference    (Z. Naturforsch. 30c, 516—519 [1975]; eingegangen am 29. November 1974/22. Januar 1975) 
  Published    1975 
  Keywords    Yeast, Sphaeroplasts, mRNA, Messenger-Ribonucleoproteids 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0516.pdf 
 Identifier    ZNC-1975-30c-0516 
 Volume    30 
2Author    G. Metz, Ruth Marx, K.-H RohmRequires cookie*
 Title    The Quaternary Structure of Yeast Aminopeptidase I 1. Molecular Forms and Subunit Size  
 Abstract    The smallest active form of aminopeptidase I (EC 3.4.11.1) from yeast has a molecular weight of 6.4 X 105. At neutral pH the active enzyme is in equilibrium with two inactive subfragments (Mr = 3 .2 X 1 0 5 and 1.1 X 105) as well as with higher aggregates (Mr 1.2 X 1 0 6). All of these species may be dissociated to give a single type of subunits with a molecular weight of 5.3 X 1 0 4. It is concluded that the active enzyme is a dodecamer whereas the subfragments correspond to dimeric and hexameric forms. 
  Reference    (Z. Naturforsch. 32c, 929 [1977]; received August 2 1977) 
  Published    1977 
  Keywords    Aminopeptidase, Yeast, Structure, Subunit Composition 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0929.pdf 
 Identifier    ZNC-1977-32c-0929 
 Volume    32 
3Author    Bemd Schulz-Harder, Claudia KiichererRequires cookie*
 Title    in Saccharomyces cerevisiae  
 Abstract    The ribosomal ribonuclease of yeast is induced after a withdrawal of glucose. Cycloheximide inhibits the synthesis of the enzyme under conditions of induction but antimycin shows no effect. Hence, the increase of the ribonuclease activity during growth of yeast is due to newly synthesized enzyme, and the induction does not depend on respiration. 
  Reference    Z. Naturforsch. 35c, 168—170 (1980); received February 13/September 5 1979 
  Published    1980 
  Keywords    Yeast, Ribosomes, Ribonuclease, Cycloheximide, Antimycin 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0168_n.pdf 
 Identifier    ZNC-1980-35c-0168_n 
 Volume    35 
4Author    Bernd Schulz-Harder, Ernst-Randolf LochmannRequires cookie*
 Title    Initiation in einem Polyribosomen-abhängigen Protein-synthetisierenden zellfreien System aus Saccharomyces Initiation in a Polyribosome-Dependent Protein-Synthesizing Cell-Free System from Saccharomyces  
 Abstract    A method to prepare polyribosomes from yeasts by using the french-press is described. The highest yield of polyribosomes was derived from late log-phase cells. These polyribosomes, in­ cubated in a cell-free system, were able to reinitiate protein synthesis, which was shown by in­ hibiting aminoacid incorporation by aurintricarboxylic acid, edeine and sodiumfluoride. W e de­ veloped the translational system in order to look for the optimal ion-conditions of a DNA-dependent protein-synthesizing system. W e found out that at the optimal MgCL-concentration (6 mM) protein synthesis was strongly inhibited by Mangan ions which are required for transcription in yeast. If protein-synthesis was carried out with 2 mM and 3 mM M gCU maximal aminoacid incorporation was observed at 2 mM and 1.5 mM M nCl2 . 
  Reference    (Z. Naturforsch. 31c, 169 [1976]; eingegangen am 10. November 1975) 
  Published    1976 
  Keywords    Yeast, Polyribosomes, Cell-Free Protein Synthesis, Antibiotics, Ion-Conditions 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0169.pdf 
 Identifier    ZNC-1976-31c-0169 
 Volume    31 
5Author    Brigitte Kiefer, LaskeRequires cookie*
 Title    Jürgen  
 Abstract    Protein synthesis after UV-and X-irradiation was investigated in diploid yeast. The incorpora­ tion of radioactively labelled lysine and phenylalanine was measured 2.5 and 4 hours after ex­ posure. By varying the specific activity the pool sizes could be estimated. At 2.5 hours there is some increase in pool sizes and a dose-dependent enhancement of protein synthesis. At 4 hours pools are again normal, but the increase of synthetic activity prevails. 
  Reference    (Z. Naturforsch. 32c, 973 [1977]; received August 29 1977) 
  Published    1977 
  Keywords    Yeast, Protein Synthesis, Amino Acid Pools, Irradiation 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0973.pdf 
 Identifier    ZNC-1977-32c-0973 
 Volume    32 
6Author    J.F T Spencer, DorothyM. SpencerRequires cookie*
 Title    Osmotic Sensitivity and Tolerance and Proteinase Production in a Strain of Saccharomyces  
 Abstract    A brewing yeast strain, NCYC 1085, unusual in that it sporulated freely and produced diploid spores, was sensitive to the degree of osmotic tension induced by the addition of 1.5 M KC1 or 2.5 m ethylene glycol to yeast extract-peptone-glucose medium, but its progeny, obtained on sporula-tion and dissection of the resulting asci, included a number of osmotic-tolerant strains, the per­ centage of which increased as these strains were also sporulated and dissected. In addition, after repeated isolation of single-spore clones for three or four generations, clones producing zones of liquefaction of gelatin ranging in size from zero to large (approximately 1.5 cm) appeared, with the intensity of hydrolysis increasing in clones obtained from the later generations. The isolation of erythromycin-resistant mutants by manganese treatment was also accompanied by the appearance of osmotic-tolerant and gelatin-liquefying clones. 
  Reference    Z. Naturforsch. 34c, 131 (1979); received November 5 1978 
  Published    1979 
  Keywords    Yeast, Saccharom yces, Extracellular Proteases, Genetics, Osmotolerance 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0131.pdf 
 Identifier    ZNC-1979-34c-0131 
 Volume    34 
7Author    Maja Mischel, Ingolf LamRequires cookie*
 Title    Dielectrophoretic Rotation in Budding Yeast Cells  
 Abstract    Rotation of budding yeast cells in an alternating non-uniform electric field of low frequency was investigated. Rotation frequency was found to be proportional to field strength above a threshold, and varied from cell to cell. The threshold is inversely correlated with the mom ent of inertia of the cells, while the slope of rotation frequency versus field strength increases with the moment. Rotation frequencies varied between 1 and 10 cycles per second. Clear differences between the dielectrophoretic behaviour o f living and heat-inactivated yeast cells were observed. 
  Reference    Z. Naturforsch. 35c, 1111 (1980); received July 21/Septem ber 10 1980 
  Published    1980 
  Keywords    Dielectrophoresis, Rotation, Yeast, N onuniform Electric Fields 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-1111_n.pdf 
 Identifier    ZNC-1980-35c-1111_n 
 Volume    35 
8Author    Christian KreutzfeldtRequires cookie*
 Title    Initiation of Protein Synthesis in Yeast: Binding of Met-tRNAj  
 Abstract    Conditions for the binding of Met-tRNAj to 40 s ribosomal subunits and to proteins isolated out o f the yeast ribosomal KC1 wash were investigated. Sucrose density gradient experiments revealed that binding of Met-tRNAj to 40 s ribosomal subunits was catalyzed in a AUG and GTP dependent reaction. Binding of Met-tRNAi to proteins of the ribosomal KC1 wash as assayed by the Millipore filter technique was found to be independent of AUG, GTP and 40 s ribosomal subunits. Additions of GTP yielded only slight stimulation, whereas Mg2+ caused dissociation of complexes. It was concluded that these reactions were most likely catalyzed by initiation factor eIF-2 although stimulation by GTP did not occur. 
  Reference    Z. Naturforsch. 36c, 142—148 (1981); received September 18 1980 
  Published    1981 
  Keywords    Protein Synthesis, Initiation, Initiator tRNA, Yeast 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0142.pdf 
 Identifier    ZNC-1981-36c-0142 
 Volume    36 
9Author    Hans-Jürgen Schuetz, H. Elm, Ut SimonRequires cookie*
 Title    Degradation of NAD(H ) by Endogenous Enzymes of Yeasts and Clostridia  
 Abstract    The time courses of degradation of exogenous NAD and NADH (2.5 m M) catalyzed by en­ dogenous enzymes present in Saccharom yces cerevisiae, Candida utilis, Clostridium spec. La 1, C lostridium kluyveri, and Clostridium sporogenes have been determined. The half lives of the pyridine nucleotides depend extremely on the organism and, for the same organism, on the growth conditions. C. spec. La 1 as well as C. kluyveri possess only negligible enzyme activities for NAD degradation. However, C. sporogenes shows activities leading to half lives of less than 2 h for NAD and 5 h for NADH. At 25 °C half lives in the order of 5 — 17 h have been observed for Candida utilis under different conditions. The half lives of NAD are roughly 5 times higher in the presence of Saccharom yces cerevisiae. 
  Reference    Z. Naturforsch. 41c, 172—178 (1986); received July 25. 1985 
  Published    1986 
  Keywords    NAD(H) Degradation, Clostridia, Yeasts, Bioconversion, Enzymatic Reductions 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0172.pdf 
 Identifier    ZNC-1986-41c-0172 
 Volume    41 
10Author    Susana Raquel, Correa Garcia, MariaVictoria Rossetti, Alcira Maria, Carmen Batlle, Porfirinas, Porfirias-C Ip, Y. P., N. Ic, E. T., F.C E, N.Requires cookie*
 Title    Studies on Porphobilinogen-Deaminase from Saccharomyces cerevisiae  
 Abstract    Porphobilinogen-deaminase from Saccharomyces cerevisiae has been isolated and partially purified 80-and 230-fold in the absence or presence o f phenylmethylsulphonyl fluoride, re­ spectively. Some properties o f the isolated enzyme were studied. Porphyrin formation was linear with time and protein concentration. O ptim um pH was about 7.5-7.8. Molecular mass o f the pro­ tein was 30,000 ± 3000 Dalton when the enzyme was purified in the presence o f phenylmethyl­ sulphonyl fluoride. A less active and unstable 20,000 D a molecular mass species was obtained when purification was performed in the absence o f the protease inhibitor. Porphobilinogen-deaminase exhibited classical Michaelis-Menten kinetics. The apparent Ky for uroporphyrinogen formation was 19 hm; Fmax was 3.6 nmol uroporphyrin/h and the Hill coefficient was n = 1. Also the action o f several reagents on the activity was studied. Protective thiol agents had no effect. Heavy metals inhibited both porphyrin formation and porphobilinogen consumption, but known sulphydryl inactivating chemicals inhibit the former without modifying the latter. A m m o nium ions had no effect on the activity while hydroxylamine completely inhibited both porphyrin form ation and porphobilinogen consumption. 
  Reference    Z. Naturforsch. 46c, 1017—1023 (1991); received December 17 1990/May 27 1991 
  Published    1991 
  Keywords    Saccharomyces cerevisiae, Yeast, Porphobilinogen-Deaminase, Porphyrin Biosynthesis, Porphobilinogen 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-1017.pdf 
 Identifier    ZNC-1991-46c-1017 
 Volume    46 
11Author    G. Alina Lazarova, Tam Otsu, O. Otaki, Kunio Isono, H. Ironao, K. AtaokaRequires cookie*
 Title    Phototropism in Yeast: A New Phenomenon to Explore Blue Light-Induced Responses  
 Abstract    Although yeasts have been intensively investigated in photobiology, directional response of yeast growth to light has never been observed. The present data demonstrate for the first time phototropism in yeast, the basidiomycetous yeast Sporobolomyces salmonicolor. The effective spectral band is blue light -suggesting that a blue-light receptor similar to that in other plants is involved in yeast photophysiology. Further studies on yeast phototropism could help identification of the photoreceptor and throw new light on the mechanisms of signal transduction and response. 
  Reference    Z. Naturforsch. 49c, 751—756 (1994); received July 19 1994 
  Published    1994 
  Keywords    Phototropism, Yeast, Sporobolomyces salmonicolor, Blue Light 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0751.pdf 
 Identifier    ZNC-1994-49c-0751 
 Volume    49 
12Author    M. Auro, Sola-Pennaa, JoseR. Oberto, M. Eyer-FernandesbRequires cookie*
 Title    Trehalose Protects Yeast Pyrophosphatase against Structural and Functional Damage Induced by Guanidinium Chloride  
 Abstract    Trehalose is accumulated at very high concentrations in yeasts when this organism is sub­ mitted to a stress condition. This report approaches the question on the protective effect of trehalose and its degradation product, glucose, against structural and functional damage promoted by guanidinium on yeast cytosolic pyrophosphatase. Here it is shown that both, 1 m trehalose or 2 m glucose, are able to attenuate at almost the same extent the conforma­ tional changes promoted by guanidinium chloride on the pyrophosphatase structure. On the other hand, while 1 m trehalose increases 3.8 times the K x (from 0.15 to 0.57 m) for guanidi­ nium chloride inhibition of pyrophosphatase activity, 2 m glucose did not even duplicate this parameter (from 0.15 to 0.25 m). These data support evidences for a functional reason for the accumulation by yeasts of trehalose, and not other compound, during stress conditions. 
  Reference    Z. Naturforsch. 51c, 160—164 (1996); received September 15/November 15 1995 
  Published    1996 
  Keywords    Trehalose, Yeast, Carbohydrate, Protection, Guanidinium Chloride 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0160.pdf 
 Identifier    ZNC-1996-51c-0160 
 Volume    51 
13Author    Hans Eckstein, Sybille Ahnefeld, Karin Albietz-LogesRequires cookie*
 Title    Synthesis of Deoxynucleoside Tri-and Monophosphates in Synchronized and Asynchronously Growing Cells Acid-Soluble Deoxynucleotides and DNA Synthesis in Growing Yeast after X-Irradiation, II  
 Abstract    The behaviour of acid-soluble D NA precursors in synchronized and asynchronously growing yeast after X-irradiation is investigated by labeling techniques with 32P; and by enzymic estimation. In prelabeled synchronized growing cells, radioactivity associated with deoxynucleoside triphos­ phates increases to maximum values shortly before each DNA replication, followed by a drastic decrease during S-phase. Radioactivity associated with monophosphates fluctuates, too, but with an opposite rhythm. These fluctuations apparently reflect quantitative changes of the DNA precursor pool during a cell cycle, as judged from the following findings: 1. Acid-soluble phosphorus is augmented stepwise. 2. "Specific" radioactivity from acid-soluble phosphorus compounds de­ creases steadily, indicating a continuous dilution of the labeled phosphorus pool with "cold" phos­ phorus. 3. Radioactivity associated with ribonucleotides fluctuates, too, but with a divergent rhythm. In X-irradiated synchronice growing yeast, the fluctuations of the deoxynucleotide-associated 32P are disturbed only little. Maximum values appear nearly at the same time as in the control, they decrease to minor values even if D NA augmentation is delayed. This decrease is less drastic, however, than that during DNA replication in unirradiated yeast, yielding a slightly increased aver­ age label per generation time. At the same sime a rapid augmentation of monophosphate label is observed. A pronounced increase of deoxynucleotide-32P is seen with X-irradiated asynchronously growing yeast, pointing to distinct radiosensitivities of the D N A /D N A precursor system in different cell stages. Neither 32P-fluctuations nor 32P-accumulation during DNA delay can be explained by cor­ responding observations with acid-soluble phosphorus or with ribonucleotide pools. Studies on 32P-incorporation also exclude radiation effects on cellular phosphorus uptake. Enzymic estimations of the deoxynucleoside triphosphate pools from asynchronously growing yeast rather exhibit a con­ siderable increase of these substances during the radiation-induced delay of DNA augmentation. This accumulation of DNA precursors probably is caused by undisturbed synthesis, but reduced incorporation into DNA. The possible role of D NA repair in this system is discussed. 
  Reference    (Z. Naturforsch. 29c, 272 [1974]; received January 17 1974) 
  Published    1974 
  Keywords    Deoxynucleoside Triphosphates, Deoxynucleoside Monophosphates, Yeast, X-Irradiation, Phosphorus Turnover 
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 TEI-XML for    default:Reihe_C/29/ZNC-1974-29c-0272.pdf 
 Identifier    ZNC-1974-29c-0272 
 Volume    29 
14Author    Stefan PostiusRequires cookie*
 Title    In vivo Evidence for a Functional Glycolytic Compartment in Synchronous Yeast Cells  
 Abstract    The different metabolic behaviour of endogenously produced [1-14C] pyruvate derived from [3,4-14C]glucose and of exogenously added [1-14C]pyruvate were studied with synchronous yeast cell populations, under conditions which differentially influenced the activities o f pyruvate decarboxylase in the cytoplasm and pyruvate dehydrogenase in the mitochondria. Endogenously produced [1-14C]pyruvate is decarboxylated almost exclusively by PDC under anaerobic condi­ tions, in contrast to added [1-14C]pyruvate which is decarboxylated under aerobic conditions by the action of PDH mainly. Whereas 14C 0 2 evolution from exogenous [l-14C]pyruvate can be diluted proportionally by addition o f pyruvate, this is not the case for 14C 0 2 evolution from endogenous [1-14C]pyruvate. It is suggested that glycolysis or at least some constituents o f it might be arranged in such a manner that the resulting complex behaves as a functional compartment, meaning that it is almost inaccessible to exogenously added pyruvate. 
  Reference    Z. Naturforsch. 36c, 615—6 (1981); received November 20 1980/January 28 1981 
  Published    1981 
  Keywords    Continuous 14C 0 2 Evolution, Glycolytic Compartment, Pyruvate Metabolism, Synchronous, Yeast 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0615.pdf 
 Identifier    ZNC-1981-36c-0615 
 Volume    36 
15Author    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 
16Author    Hans-Peter Hanssen, Ewald Sprecher, AndreasK. LingenbergRequires cookie*
 Title    Accumulation of Volatile Flavour Compounds in Liquid Cultures of Kluyveromyces lactis Strains  
 Abstract    The accumulation o f volatile flavour constituents in liquid cultures o f three Kluyverom yces lactis strains was studied after cultivation on defined culture m edia containing glucose as carbon source, yeast extract, vitamines, and different additional nitrogen com pounds. Besides short-chain alcohols and esters (fruit esters), 2-phenylethyl alcohol, phenylacetaldehyde, and 2-phenylethyl esters could be identified by gas chrom atography and coupled gas chrom atog-raphy-mass spectrometry. Although the com position o f these com pounds was qualitatively comparable within the three strains investigated, quantitative differences were significant and strain-dependent reactions to the culture m edium could be observed. 
  Reference    Z. Naturforsch. 39c, 1030—1033 (1984); received July 2/A ugust 28 1984 
  Published    1984 
  Keywords    Kluyveromyces lactis, Yeast, Volatiles, Flavour Com pounds, Culture C onditions 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1030.pdf 
 Identifier    ZNC-1984-39c-1030 
 Volume    39 
17Author    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 
18Author    Hans EcksteinRequires cookie*
 Title    Evidence for Cyclic GMP in the Yeast Saccharomyces cerevisiae, and Studies on Its Possible Role in Growth  
 Abstract    The yeast Saccharomyces cerevisiae is shown to be equipped with cyclic GMP, the level of which ranges from 6 pmol/10 9 cells with pressed baker's yeast to 21 pmol/10 9 cells with exponentially growing cells. In extracts from synchronized growing yeast, cyclic GMP increases stepwise, being doubled at the time of each mitosis. Theophylline and 3-isobutyl-l-methylxanthine induce a rapid increase of cyclic GMP, followed by a premature formation of the septal cell wall between mother cell and bud. The effects of 3-isobutyl-l-methylxanthine are reversible. Dibutyryl-cyclic GMP, and, after a pronounced lag, also dibutyryl-cyclic AMP, induce a premature cell division, too. Cholera toxin induces premature cell divisions without a preceding increase in cyclic GMP. Neither theophylline nor 3-isobutyl-l-methylxanthine, cholera toxin or one of the dibutyryl-cyclic nucleotides modify the growth rate of the culture. None of the agents has significant effects on the level of cyclic AMP. The results suggest that cyclic GMP possibly controls an early step of mitosis, whereas ADP-ribosylation might govern a subsequent event. 
  Reference    Z. Naturforsch. 43c, 386—396 (1988); received October 20 1987 
  Published    1988 
  Keywords    Cyclic GMP, Cyclic AMP, Phosphodiesterase Inhibitors, Cholera Toxin, Growth, Yeast 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0386.pdf 
 Identifier    ZNC-1988-43c-0386 
 Volume    43 
19Author    FranciscoF. De, La Rosa, Graham PalmerRequires cookie*
 Title    Anomalous Reduction of Cytochrome b in Highly Purified Complex III from Baker's Yeast  
  Reference    Z. Naturforsch. 37c, 445—4 (1982); received November 26 1981 
  Published    1982 
  Keywords    Cytochrome b, Anomalous Reduction, "Control Factor", Yeast, Highly Purified fo-Complex 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0445.pdf 
 Identifier    ZNC-1982-37c-0445 
 Volume    37