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Facet   Publication Year 1988  [X]
Facet   section ZfN Section C:Volume 043  [X]
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1988[X]
21Author    Manfred Wiegand, Karl EiseleRequires cookie*
 Title    Isolation and Characterization of the Androgen Receptor of Murine Preputial Gland  
 Abstract    The androgen receptor of murine preputial gland showed in binding experiments a biphasic saturation curve and a biphasic Scatchard plot. The receptor converted from an 8.5-9 S form to a 4.5—5 S form in high ionic strength buffer. The apparent dissociation constant was K D 0.5 ± 0.2 nM for the 8.5—9 S receptor form. A 6.5—7 S receptor form could be detected in some experiments. The ligand specificity was evaluated by competition experiments: testosterone > androstene-dione > dihydrotestosterone > androstanediol > estradiol > progesterone > dexamethasone. The receptor of murine preputial gland was less stable than the androgen receptor of skeletal muscle of the same mice. 
  Reference    Z. Naturforsch. 43c, 117—125 (1988); received September 25 1987 
  Published    1988 
  Keywords    Murine Preputial Gland, Androgen Receptor, Isolation, Characterization 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0117.pdf 
 Identifier    ZNC-1988-43c-0117 
 Volume    43 
22Author    Karlheinz Tempel, Rüdiger HeinzelmannRequires cookie*
 Title    Sedimentation von Nukleoiden aus Thymus-und Milzzellen der Ratte nach Ganzkörper-Röntgenbestrahlung Sedimentation of Nucleoids from Thymic and Splenic Cells of the Rat Following Total-Body X-Irradiation  
 Abstract    The sedimentation of nucleoids from thymic and splenic cells of rats was tested following total-body X-irradiation (TBI) with doses ranging from 24 to 1520 cGy. The principal results may be summarized as follows: 1) The nucleoid sedimentation of the cells was reduced immediately after TBI with doses of > 760 cGy. In the following postirradiation period, an enhancement of sedimentation rate has been observed which could be neutralized by addition of proteinase K to the nucleoid preparation. 2) When nucleoids were prepared 6 h after TBI with doses > 190 cGy, beside the main nucleoid band a smaller nucleoid fraction appeared in the ethidium bromide containing saccharose gradient. This fraction was of less sedimentability than the main nucleoid peak and could not be distinguished from pure, high molecular DNA. — From the present results it is suggested that the reduction of the nucleoid sedimentation immediately following high doses of TBI is the result of primary (non-repaired) DNA lesions whereas the changes detectable some hours later are due to the secondary enzymatic changes connected with the interphase death of the cells. With respect to the detection of in vivo effects of X-irradiation, the nucleoid sedimentation has to be regarded much less sensitive than some biochemical and/or cytomorphological methods. 
  Reference    Z. Naturforsch. 43c, 126—132 (1988); received August 14/October 2 1987 
  Published    1988 
  Keywords    X-Irradiation, Rat Thymic Cells, Rat Splenic Cells, Nucleoids, DNA-Protein-Cross-links 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0126.pdf 
 Identifier    ZNC-1988-43c-0126 
 Volume    43 
23Author    Bernhard HuchzermeyerRequires cookie*
 Title    Nucleotide Binding and ATPase Activity of Membrane Bound Chloroplast Coupling Factor (CFj)  
 Abstract    of Inactivation It has been found that the decay of light triggered ATPase activity is paralleled by non-exchangeable type of binding of one ADP per mol of CF,. Inactivation of light triggered ATPase activity is a continuous process. It can be described mathematically as shown in this paper. Three simplified reaction schemes are described, each of them describing the mode of ATPase inactiva-tion in a mechanistic way. A computer simulation of each model was performed and the results were compared to the observed experimental data. In the presence of phosphate our results were explained best by a model assuming that there is at first a rapid binding of ADP to "exchangeable" sites. Due to a slowly occurring change in the CF, protein with prolonged incubation, an increasing portion of the nucleotides can be found bound in a non-exchangeable way after some seconds of incubation. Our model does not rule out that this reaction sequence might be a part of a catalytic cycle in vivo. — Another result was the finding that there is an additional diminution of ATPase activity when phosphate is lacking. 
  Reference    Z. Naturforsch. 43c, 133—139 (1988); received June 19 1987 
  Published    1988 
  Keywords    Chloroplasts, CF 0 CF, Light Triggered ATPase Activity, Regulation Mechanism 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0133.pdf 
 Identifier    ZNC-1988-43c-0133 
 Volume    43 
24Author    Wilhelm Hasselbach, Andrea MigalaRequires cookie*
 Title    Interaction of Ryanodine with the Calcium Releasing System of Sarcoplasmic Reticulum Vesicles  
 Abstract    Heavy sarcoplasmic reticulum vesicles were reacted with ryanodine in 0.6 M KCl 0.3 M sucrose at pH 6.3 and pH 7.0 at 20 °C. The inhibition of caffeine induced calcium release from actively loaded vesicles by ryanodine was applied to monitor time course and attainment of equilibrium of the interaction of ryanodine with its receptors in the vesicular membranes. At ryanodine concentrations rising from 0.1-100 | XM, the logarithms of the release amplitudes linearly decline with time. The dependence of the inactivation reaction on the concentration of ryanodine did not saturate in the applicable concentration range. The reaction halflife times are concentration dependent. At pH 7.0, the half times decline from 100 to 10 s when the ryanodine concentration is raised from 0.1 to 1 [J, M. At pH 6.3 a corresponding decline occurs between 3 (XM and 100 | AM. The marked dependence of the inactivation reaction on medium pH requires reaction times of one and five hours at pH 7.0 and 6.3, respectively for the attainment of reaction equilib-rium at low ryanodine concentrations. The dependence of the amplitude of calcium release on the concentration of added ryanodine has been evaluated as proposed by Gutfreund (Enzymes: Physical Principles, p. 71, Wiley-Interscience, London 1972) for the preparation's affinity for ryanodine and its number of binding sites. At pH 7.0, preparations appear to contain only 0.7 pmol sites per mg protein having an affinity for ryanodine of 0.33 nM"'. The titration curves for caffeine induced calcium release, initial calcium uptake and final calcium level are identical, indicating that the three functions are controlled by the same receptor. Calcium induced calcium release, however, is only partially and differently affected by the occupancy of the high affinity ryanodine binding sites. The kinetic and equilibrium data for the effects of ryanodine were combined and analyzed on account of a two step reaction sequence. The corresponding dissociation and rate constants were evaluated and combined with reported data of [ 3 H]ryanodine binding (Pessah et al., J. Biol. Chem. 261, 8643-8648 (1986)). 
  Reference    Z. Naturforsch. 43c, 140—148 (1988); received November 4 1987 
  Published    1988 
  Keywords    Sarcoplasmic Reticulum Ryanodine, Caffeine, Calcium Release 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0140.pdf 
 Identifier    ZNC-1988-43c-0140 
 Volume    43 
25Author    H.Oskar SchmidtRequires cookie*
 Title    The Structure and Function of Grana-Free Thylakoid Membranes in Gerontoplasts of Senescent Leaves of Vicia faba L  
 Abstract    In the course of yellowing (senescence) the leaves of Vicia faba L. lose 95% of their chlorophyll. Gerontoplasts develop from chloroplasts and aggregate with the pycnotic mitochon-dria and the cell nucleus in the senescent cells (organelle aggregation). The gerontoplasts contain only a few, unstacked thylakoid membranes but a large number of carotinoid-containing plasto-globuli, which after the degration of chlorophyll presumably assume the light protection of the cells. The thylakoid membranes of the gerontoplasts were isolated by means of a flotation method. Their polypeptide composition is characterized by a high proportion of light-harvesting complex. Evidence of relatively high photochemical activity shows that functional thylakoid mem-branes are present in the premortal senescence state of leaves and this suggests that there is functional compartmentation of the hydrolytic processes in this stage of the leaves' development. 
  Reference    Z. Naturforsch. 43c, 149—154 (1988); received March 11/September 7 1987 
  Published    1988 
  Keywords    Senescence, Chloroplast, Gerontoplast, Thylakoid Membrane Proteins, Electronmicroscopy, Photosynthesis 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0149.pdf 
 Identifier    ZNC-1988-43c-0149 
 Volume    43 
26Author    DrBernhard WolfRequires cookie*
 Title    Elektronen-Energie-Verlust-Spektroskopische Untersuchungen an Luftfiltern zur Bewertung der Luftqualität Electron-Energy-Loss-Spectroscopical Investigations on Air Filters for the Analysis of the Air Quality  
 Abstract    In trace analysis it is more and more attempted to replace wet-chemical detection procedures by methods which allow a quantitative analysis without any material disintegration, but on exploiting the characteristic physical properties of the components searched for. Based on a procedure for physical and biological valuation of the air quality by means of X-ray microanalysis (WDX/EDX), a procedure which was previously developed by our group, we deepened our investigations by the help of electron-energy-loss-spectroscopy (EELS). The combination of that procedure with EELS proved to be very advantageous as it revealed a high sensitivity as well as a high energy resolution. The main advantages are to be found in the simple arrangement of the sample detector and in the fact, not only being able to examine deposits microscopically, but also to analyze them chemically without disintegrating the material. Thus loss of material and denaturation are largely excluded. 
  Reference    Z. Naturforsch. 43c, 155—161 (1988); received November 4 1987 
  Published    1988 
  Keywords    Air Analysis, Filter Detection, Electron Microscopy, Electron-Energy-Loss-Spectroscopy 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0155.pdf 
 Identifier    ZNC-1988-43c-0155 
 Volume    43 
27Author    J. Paul, E. V. Goldammer, H. R. WenzelRequires cookie*
 Title    Pressure Induced Structural Fluctuations in Hemoglobin, Studied by EPR-Spectroscopy  
 Abstract    A quartz based cavity for pressure dependent EPR measurements on liquid samples allowing pressures up to 0.6GPa was constructed. First investigations with this setup were done on spin labeled horse hemoglobin derivatives both in ferric and ferrous state of oxidation. The second derivative EPR spectra show changes of the label's mobility, which are not correlated with spin state changes of the Fe-porphyrin complex, but which point out structural fluctuations inside the globin protein matrices. 
  Reference    Z. Naturforsch. 43c, 162—166 (1988); received December 22 1987 
  Published    1988 
  Keywords    High-Pressure, Electron Paramagnetic Resonance, Second Harmonic Detection, Liquid Systems, Hemo-Proteins, Structural Fluctuation, Ligand Binding 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0162.pdf 
 Identifier    ZNC-1988-43c-0162 
 Volume    43 
28Author    Peter Schmidt, Reiner Kühlmann, Uli LöschRequires cookie*
 Title    A Competitive Inhibition Enzyme Immunoassay for Detection and Quantification of Organophosphorus Compounds  
 Abstract    A sensitive and specific method for detection and quantification of methyl phosphonic acid, p-aminophenyl 1,2,2,-trimethyl-propyl diester (MATP) as a model substance for organophosphorus compounds is described. Different procedures for coupling the haptenic group for immunization, purification and im-mobilization allowed the detection of hapten-specific antibodies. The competitive inhibition enzyme immunoassay (CIEIA), using purified chicken and rabbit IgG-antibodies, was able to detect MATP-concentrations as low as 1(T 10 mol/1. Based upon our results, we postulate that the CIEIA represents a good alternative to the customary diagnosis of organophosphate intoxications, measuring blood Cholinesterase activity. 
  Reference    Z. Naturforsch. 43c, 167—172 (1988); received November 24 1987 
  Published    1988 
  Keywords    ELISA, Haptens, Organophosphorus Agents 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0167.pdf 
 Identifier    ZNC-1988-43c-0167 
 Volume    43 
29Author    Paul-Gerhard Gülz, Edith Müller, Brigitte MoogRequires cookie*
 Title    Epicuticular Leaf Waxes of Tilia tomentosa Moench. and Tilia X europaea L., Tiliaceae  
 Abstract    Tilia tomentosa Moench., T. x europaea L., Epicuticular Leaf Wax Composition, ß-Amyrin Free and Esterified Quantity and composition of epicuticular leaf wax of Tilia tomentosa Moench. and T. x europaea L. were examined and showed similar wax compositions. The waxes of these two Tilia species contained homologous series of n-alkanes, wax esters, aldehydes, acetates, primary al-cohols and fatty acids. In addition to these common epicuticular wax constituents, the triterpenol ß-amyrin was found free as well as esterified with long chain fatty acids and in very high amounts with acetic acid in both Tilia species. 
  Reference    Z. Naturforsch. 43c, 173—176 (1988); received December 28 1987/January 28 1988 
  Published    1988 
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 Identifier    ZNC-1988-43c-0173 
 Volume    43 
30Author    A. Stärk, T. Anke, A. Kirfel, G. WillRequires cookie*
 Title    Lentinellic Acid, a Biologically Active Protoilludane Derivative from Lentinellus Species (Basidiomycetes) [1]  
 Abstract    A new antimicrobial and cytotoxic sesquiterpenoid, lentinellic acid (1), has been isolated from submerged cultures of Lentinellus ursinus and L. omphalodes. The structure of the antibiotic was elucidated by spectroscopic methods and a single crystal X-ray analysis. 1 may be formed biogenetically by condensation of a protoilludane aldehyde 4 with a malonate unit. 
  Reference    Z. Naturforsch. 43c, 177—183 (1988); received October 16 1987 
  Published    1988 
  Keywords    Lentinellus, Basidiomycetes, Sesquiterpenoids, Protoilludanes, Lentinellic Acid, Antibiotics 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0177.pdf 
 Identifier    ZNC-1988-43c-0177 
 Volume    43 
31Author    J. Tripathi, T. JoshiRequires cookie*
 Title    Phytochemical Investigation of Roots of Pterocarpus marsupium. Isolation and Structural Studies of Two New Flavanone Glycosides  
 Abstract    From the roots of Pterocarpus marsupium 7-Hydroxy-6, 8-dimethyl flavanone-7-O-a-L-arabino-pyranoside and 7,8,4'-trihydroxy-3', 5'-dimethoxy flavanone-4'-0-ß-D-glucopyranoside have been isolated and their structure elucidated. 
  Reference    Z. Naturforsch. 43c, 184—186 (1988); received July 2 1987/January 13 1988 
  Published    1988 
  Keywords    Pterocarpus marsupium, Leguminosae, Flavanone Glycosides 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0184.pdf 
 Identifier    ZNC-1988-43c-0184 
 Volume    43 
32Author    Margot Schulz, Gottfried WeissenböckRequires cookie*
 Title    Dynamics of the Tissue-Specific Metabolism of Luteolin Glucuronides in the Mesophyll of Rye Primary Leaves (Secale cereale)  
 Abstract    Developing primary leaves of Secale cereale L. exhibit a dynamic metabolism of the major flavonoid luteolin 7-0-[ß-D-glucuronosyl(l—»2)ß-D-glucuronide]-4'-0-ß-D-glucuronide (Ri). Fi-nal steps of R, biosynthesis are sequential glucuronidations of luteolin, which are catalyzed by three specific UDP-glucuronate: flavone glucuronosyltransferases. These enzymes reach highest activities at the fourth and fifth day of leaf development, coinciding with maximal R, accumula-tion. The activities decrease with advancing age of the leaves. In contrast, a R,-specific ß-glucuronidase, responsible for the hydrolysis of glucuronic acid in position 4', shows increasing activity up to the 5 th or 6 th day; but this activity, leading to luteolin 7-O-diglucuronide (R 2), is not reduced in later developmental stages. In this phase of leaf development, the amount of R, drastically drops, whereas R 2 accumulates only slightly. From in vitro results and from feeding experiments using [ 14 C]cinnamic acid, a precursor of R, biosynthesis, we conclude that the anabolic sequential glucuronidation takes place in young and expanding leaf tissue, whereas deglucuronidation occurs in nearly mature and mature tissue. The three glucuronosyltransferases as well as the ß-glucuronidase, and the flavonoids R) and R 2 are localized in the mesophyll. 
  Reference    Z. Naturforsch. 43c, 187—193 (1988); received November 19/December 30 1987 
  Published    1988 
  Keywords    Secale cereale L, UDP-glucuronate: flavone-glucuronosyltransferases, ß-Glucuronidase, Luteolin 7-0-Diglucuronosyl-4'-0-Glucuronide 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0187.pdf 
 Identifier    ZNC-1988-43c-0187 
 Volume    43 
33Author    Matthias Höpfner, Georg Reifferscheid, Aloysius WildRequires cookie*
 Title    Molecular Composition of Glutamine Synthetase of Sinapis alba L  
 Abstract    Chloroplastic glutamine synthetase of Sinapis alba, purified to homogeneity by a simple three step procedure, revealed a molecular weight of about 395 kDa. The native enzyme is composed of eight subunits of identical molecular weight (about 50 kDa (each), although isoelectrofocusing yielded six distinct bands in the pH 5.6 region of the gel. Labelling of the enzyme with the glutamate analogue herbicide [ 14 C]phosphinothricin and with [y-32 P]ATP indicated that glutamine synthetase has eight reactive centers per molecule. The native enzyme dissociated into two enzymatically active subaggregates of about 195 kDa after Mg 2+ deprivation. 
  Reference    Z. Naturforsch. 43c, 194—198 (1988); received November 26 1987 
  Published    1988 
  Keywords    Active Centers, Enzyme Purification, Enzyme Structure, Glufosinate, Glutamine Synthetase, Phosphinothricin 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0194.pdf 
 Identifier    ZNC-1988-43c-0194 
 Volume    43 
34Author    Maike Petersen, Ulrich Hanns, Seitz, Ernst ReinhardRequires cookie*
 Title    Characterization and Localization of Digitoxin 12 ß-Hydroxylase from Cell Cultures of Digitalis lanata EHRH  
 Abstract    The cytochrome P-450-dependent monooxygenase digitoxin 12ß-hydroxylase from cell cultures of Digitalis lanata needs NADPH and molecular oxygen and hydroxylates cardiac glycosides with the aglycon of digitoxigenin to the corresponding derivatives of the C-series. Other electron donors cannot replace NADPH. The apparent K" m -values are 26 UM for NADPH, 7.1 ^IM for ß-methyldigitoxin and 10 ^IM for digitoxin. The reaction is inhibited by NADP + and cytochrome c in a competitive mode. The optimum temperature was at 20 °C. Low concentrations of Mn 2+ , Mg 2+ , and EDTA were slightly stimulatory, but there was no strict dependence on divalent cations. Digitoxin 12ß-hydroxylase is very stable at room temperature and the reaction proceeds for more than 20 h. After the addition of 15% glycerol, 70% of the original activity can be retained subsequent to freezing at —18 °C. By means of linear sucrose gradient fractionation of cellular membranes the digitoxin 12ß-hydroxylase was found to be located in the endoplasmic reticulum. 
  Reference    Z. Naturforsch. 43c, 199—206 (1988); received December 8 1987 
  Published    1988 
  Keywords    Cardiac Glycosides, Cytochrome P-450, Digitalis lanata, Digitoxin 12ß-Hydroxylase, Endoplas-mic Reticulum 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0199.pdf 
 Identifier    ZNC-1988-43c-0199 
 Volume    43 
35Author    Roland Pschorn, Wolfgang Rühle, Aloysius WildRequires cookie*
 Title    The Influence of the Proton Gradient on the Activation of Ferredoxin-NADP + -oxidoreductase by Light  
 Abstract    Ferredoxin-NADP + -oxidoreductase (FNR, EC 1.18.1.2) has been shown to be activated by light within a few seconds during dark-light transitions and inactivated in the dark. In previous papers this could be pointed out by the correlation of cytochrome /induction kinetics to the rate of NADP-photoreduction and the variable fluorescence. The present study deals with the role of the proton gradient during the activation process. The transition from an inactive to an active form is followed continuously in an in situ system. The steady-state rate of NADP-photoreduction is affected only by ionophores which inhibit a formation of the proton gradient, but not by inhibitors of the electric field. It correlates to the 9-aminoacridine fluorescence quench and the light scattering signals at 535 nm. The perception of the pH-gradient through the enzyme is still a matter of discussion. 
  Reference    Z. Naturforsch. 43c, 207—212 (1988); received December 28 1987 
  Published    1988 
  Keywords    Electron Transport, Ferredoxin-NADP + -oxidoreductase, Light Activation, Proton Gradient 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0207.pdf 
 Identifier    ZNC-1988-43c-0207 
 Volume    43 
36Author    Bernhard HuchzermeyerRequires cookie*
 Title    Phosphate Binding to Isolated Chloroplast Coupling Factor (CF^  
 Abstract    A single binding site for phosphate was found on isolated chloroplast coupling factor in the absence of nucleotides. In our experiments the phosphate binding site showed a K d of 170 JIM. We did not observe any differences whether the ATPase activity of CF] had been activated or not. If the enzyme was incubated with [y-32 P]ATP the amount of 32 P bound per CF, depended on the pretreatment of the enzyme: In the presence of ADP no ATP or phosphate was bound to CF,. After activation of ATPase activity one mol of ATP per mol CF, was rapidly bound and hydro-lyzed while there was a slowly occurring binding of another phosphate without concomitant nucleotide binding. We conclude that there are two different types of phosphate binding observed in our experi-ments: 1) Inorganic phosphate can be bound by one catalytic site per mol of CTv 2) The y-phosphate of ATP is able to bind to an ATP binding domain of the enzyme if this domain can exchange substrates with the incubation medium. This ATP binding domain appears to differ from the site binding inorganic phosphate, because at least a portion of the coupling factor contains more than one labelled phosphate during our ATPase tests. 
  Reference    Z. Naturforsch. 43c, 213—218 (1988); received July 27/November 19 1987 
  Published    1988 
  Keywords    Chloroplast, Coupling Factor, Binding Sites, ATPase, Phosphorylation 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0213.pdf 
 Identifier    ZNC-1988-43c-0213 
 Volume    43 
37Author    EgbertJ. Boekema, Günter Schmidt, Peter Gräber, JanA. BerdenRequires cookie*
 Title    Structure of the ATP-Synthase from Chloroplasts and Mitochondria Studied by Electron Microscopy  
 Abstract    The structure of the ATP-synthase, F 0 F,, from spinach chloroplasts and beef heart mitochon-dria has been investigated by electron microscopy with negatively stained specimens. The deter-gent-solubilized ATP-synthase forms string-like structures in which the F 0 parts are aggregated. In most cases, the F, parts are arranged at alternating sides along the string. The F 0 part has an approximate cylindrical shape with heights of 8.3 and 8.9 nm and diameters of 6.2 and 6.4 nm for the chloroplast and mitochondrial enzyme, respectively. The F, parts are disk-like structures with a diameter of about 11.5 nm and a height of about 8.5 nm. The F, parts are attached to the strings, composed of F n parts, in most cases, with their smallest dimension parallel to the strings. The stalk connecting F 0 and F, has a length of 3.7 nm and 4.3 nm and a diameter of 2.7 nm and 4.3 nm for the chloroplast and mitochondrial enzyme, respectively. 
  Reference    Z. Naturforsch. 43c, 219—225 (1988); received December 1 1987 
  Published    1988 
  Keywords    ATP-Synthase, Enzyme Structure, Electron Microscopy 
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 Identifier    ZNC-1988-43c-0219 
 Volume    43 
38Author    S. S. BrodyRequires cookie*
 Title    The Position of Carotene in the D-l/D-2 Sub-Core Complex of Photosystem II  
 Abstract    When the sub-core complex of photosystem II, D1/D2, is irradiated at 436 or 415 nm (absorp-tion by chlorophyll and pheophytin and ß-carotene) or 540 nm (absorption primarily by pheophy-tin), the low temperature fluorescence spectrum has two maxima, at 685 and 674 nm. This shows the existence of at least two different fluorescent forms of chlorophyll (chlorophyll a and perhaps pheophytin a). When carotene is irradiated at 485 nm (absorption primarily by ß-carotene), only fluorescence at 685 nm is observed: this indicates that carotene is transferring energy to only the long-wavelength form of chlorophyll in the D1/D2 sub-core complex. The band of carotene (at 485 nm) does not appear in the fluorescence excitation spectrum, measured at 674 nm. The position of the carotene molecule relative to each of the fluorescent forms of chlorophyll was determined from the excitation spectra of each of the fluorescence bands. 
  Reference    Z. Naturforsch. 43c, 226—230 (1988); received August 21. 1987/January 11 1988 
  Published    1988 
  Keywords    Photosynthesis Photosystem II, Chlorophyll, Fluorescence, Carotenoids, Energy Transfer 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0226.pdf 
 Identifier    ZNC-1988-43c-0226 
 Volume    43 
39Author    Ryszard Stolarski, Piotr Lassota, Zygmunt Kazimierczuk, David ShugarRequires cookie*
 Title    Solution Conformations of Some Acyclo Nucleoside and Nucleotide Analogues of Antiviral Acyclonucleosides, and Their Substrate/Inhibitor Properties in Several Enzyme Systems  
 Abstract    Chemical and enzymatic procedures have been employed for the preparation of various phos-phorylated derivatives of the acyclonucleoside 9-(l,3-dihydroxy-2-propoxymethyl)adenine, an analogue of the active antiviral agent 9-(l,3-dihydroxy-2-propoxymethyl)guanine (DHPG). In combination with the previously reported 2',3'-seco nucleosides and their phosphates and cyclic phosphates (Stolarski et al., this made available a broad class of acyclonucleosides and nucleotides, the acyclic moieties of which are capable of mimicing the ribose and 2'-deoxyribose rings. The solution conformations of the foregoing were determined with the aid of 'H, 13 C and 31 P NMR, and compared with those of DHPG and 9-(hydroxyethoxymethyl)guanine (Acyclovir, ACV). Particular attention was devoted to conformations about C-O bonds in different acyclic fragments, which demonstrated well-defined differences between 2',3'-seco derivatives on the one hand (conformational "rigidity") and derivatives with DHP and AC acyclic chains on the other (rotation about the C(l')-0(4') bond). The overall results are in good general agreement with reported crystal structures, and are compared with those obtained by quantum mechanical calcu-lations. The conformational features of the various compounds are also discussed in relation to their substrate and/or inhibitor properties in a number of enzyme systems, including adenosine deamin-ase, phosphodiesterases, nuclease PI, 3'-nucleotidase and herpes virus type 1 thymidine kinase. Abbreviations: AC, 2-hydroxyethoxymethyl; DHP, 1,3-di-hydroxy-2-propoxymethyl; seco, 2',3'-seco or 1,5-dihydro-4-hydroxymethyl-3-oxapentyl-2-[R]; ACV, Acyclovir or AcycloG, 9-(2-hydroxyethoxymethyl)guanine; ACVMP, monophosphate of ACV; AC-Cyt, l-(2-hydroxyethoxy-methyl)cytosine, with similar connotations for AC-Ade and AC-Ura; DHPG, 9-(l,3-dihydroxy-2-propoxymethyl)-guanine; DHP-Ade, adenine analogue of DHPG; DHPGMP, monophosphate of DHPG; DHP-AdeMP, monophosphate of DHP-Ade; DHP-Ade-diP, 3',5'-diphosphate of DHP-Ade; DHP-Ade-3' : 5'-cMP, the 3':5'-cyclic monophosphate of DHP-Ade; secoA, 2',3'-secoadenosine or 9-(l,5-dihydro-4-hydroxymethyl-3-oxa-pentyl-2-[R])adenine, with similar connotations for other acyclonucleosides; seco-5'-GMP, 5'-monophosphate of secoG, and similarly for seco-5'-CMP and seco-5'-AMP; secoC-3' :5'-cMP, 2',3'-secocytidine-3' :5'-cyclic phos-phate, and similarly for secoA-3':5'-cMP; TK, thymidine kinase; cPDase, cyclic nucleotide phosphodiesterase. For purposes of simplicity, the abbreviated terms are used in the text, with the carbon atoms of the acyclic chains numbered as for the corresponding carbon atoms of the pentose ring, as shown in Scheme 1. 
  Reference    Z. Naturforsch. 43c, 231—242 (1988); received December 3 1987 
  Published    1988 
  Keywords    Acyclonucleosides, Phosphates, Cyclic Phosphates, Solution Conformations, Substrate/Inhibitor Properties 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0231.pdf 
 Identifier    ZNC-1988-43c-0231 
 Volume    43 
40Author    Cornelia Franzelius, Karl EiseleRequires cookie*
 Title    Interaction of Testosterone and Testosterone Receptor Complexes with Nuclei of Skeletal Muscle from Intact Male Mice and from Mice Bearing the Testicular Feminization (Tfm) Mutant Gene  
 Abstract    With the nuclear exchange assay and the nuclear retention assay it is shown that the androgen insensitivity of Tfm mice is probably due to a defect of the nuclear acceptor sites for the testos-terone receptor complex. Furtheron the results obtained point strongly to the possibility that hormone free androgen receptor is localized in the nuclei and in the cytoplasma according to the "equilibrium model". A practicable method for separation of unbound steroids from nuclei is described. 
  Reference    Z. Naturforsch. 43c, 243—248 (1988); received December 14 1987 
  Published    1988 
  Keywords    Murine Skeletal Muscle, Cell Nuclei, Testicular Feminization, Testosterone Receptor Complex, Nuclear Acceptor Sites 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0243.pdf 
 Identifier    ZNC-1988-43c-0243 
 Volume    43 
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