| 1 | Author
| Z. Naturforsch | Requires cookie* | | Title
| Isolierung und Morphologische Charakterisierung des Kartoffelblattrollvirus (PLRV)  | | | Abstract
| Isolation and M orphological Characterization o f the Potato Leafroll Virus (PLRV) J. B lessing Virologische Abteilung des Instituts für Hygiene und M ikrobiologie der U niversität des Saarlandes. H om burg/Saar, und S. S a rk a r In spite of its very low concentration, the potato leafroll virus (PLRV) can be enriched from leaf-homogenates of the infected host plant Physalis floridana by a series of separation steps and purified by ultracentrifugation through layers of cesium chloride of defined density. U nder the present experimental conditions the virus accumulates as an invisible band in a region where the density of CsCl is 1.39 ± 0.01 g/cm 3. In negatively stained preparations, the virions show a diam eter of 23 nm and some morphological criteria indicate an icosahedral symmetry. | | |
Reference
| Z. Naturforsch. 36c, 884—887 (1981); received May 23 1979/May 18 1981 | | |
Published
| 1981 | | |
Keywords
| Potato Virus, Icosahedron, Electron Microscopy | | |
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| default:Reihe_C/36/ZNC-1981-36c-0884.pdf | | | Identifier
| ZNC-1981-36c-0884 | | | Volume
| 36 | |
3 | Author
| EgbertJ. Boekema, Günter Schmidt, Peter Gräber, JanA. Berden | Requires 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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| default:Reihe_C/43/ZNC-1988-43c-0219.pdf | | | Identifier
| ZNC-1988-43c-0219 | | | Volume
| 43 | |
4 | Author
| Ulrich Schraermeyer, Hennig Stieve, Michael Rack | Requires cookie* | | Title
| Cytochemical Localization of Guanylate and Adenylate Cyclase in Photoreceptor Cells of the Fly  | | | Abstract
| In photoreceptor cells o f invertebrates light triggers an enzyme cascade in which the phos-phoinositide pathway is crucially involved. Likewise, there is growing evidence of an impor tant role of cyclic nucleotides, too. To localize these enzymes able to catalyze the formation of cGM P and cAMP, the spatial distribution of guanylate cyclase (EC 4.6.1.2) and adenylate cyclase (EC 4.6.1.1) was determined in photoreceptor cells of the fly. In photoreceptor cells of the blowfly (Calliphora erythrocephala), the electron dense reaction product o f guanylate cyclase was found within the phototransducing region, the rhabdomeral microvilli and in the mitochondria. Staining was also observed throughout the cytoplasm of the microvilli. With the same cytochemical method, reaction product for adenylate cyclase was found on the tips of the photosensory membrane, and not in the cytoplasm o f the rhabdomeral microvilli. The results presented here further argue for an important role of one or possibly two cyclic nucleotides in the photoreceptor cells, and possibly in the process o f phototransduction of in vertebrates. | | |
Reference
| Z. Naturforsch. 50c, 695—6 (1995); received May 24/July 10 1995 | | |
Published
| 1995 | | |
Keywords
| Electron Microscopy, Guanylate Cyclase, Adenylate Cyclase, Photoreceptor, Fly | | |
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| default:Reihe_C/50/ZNC-1995-50c-0695.pdf | | | Identifier
| ZNC-1995-50c-0695 | | | Volume
| 50 | |
5 | Author
| L. Raeymaekers | Requires cookie* | | Title
| The Sarcoplasmic Reticulum of Smooth M uscle Fibers  | | | Abstract
| The ability of the sarcoplasm ic (endoplasmic) reticulum (SR, ER) of smooth muscle cells to accumulate Ca was dem onstrated by measuring the uptake of 45Ca in fibers which were chemically skinned with saponin, and by electron cytochemistry of the accum ulated Ca. The Ca uptake was dependent on ATP and it was stim ulated by oxalate, as it is the case in SR of striated muscle. Electron microscopy of the skinned smooth muscle preparations revealed the presence o f calcium oxalate deposits in the reticulum . The SR vesicles were isolated from several sm ooth muscles. The purification was carried out by taking advantage o f the density increase o f the SR vesicles after loading with calcium in the presence of oxalate. Among the muscles investigated the smooth muscle of the pig stomach was found to be the most suitable and it was selected for further biochem ical and m orphological characterization of the SR vesicles. These vesicles, which contain calcium oxalate crystals, were able to accumulate an additional am ount of Ca. The Ca uptake was supported by several energy yielding substrates. T h eir order o f potency was ATP > dATP ~ U TP > ITP > G TP ~ CTP. The rate of Ca uptake was two orders o f m agnitude slower than that in SR of skeletal muscle. The measurement of the level o f phosphorylated Ca transport interm ediate showed that this difference is due to smaller num ber of calcium transport sites per vesicle. The distribution o f intram em brane particles in freeze-fractured specimens is in agreem ent with this conclusion. | | |
Reference
| Z. Naturforsch. 37c, 481—488 (1982); received January 25 1982 | | |
Published
| 1982 | | |
Keywords
| Smooth Muscle, Microsomes, Sarcoplasmic Reticulum, Calcium Metabolism, Electron Microscopy | | |
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| default:Reihe_C/37/ZNC-1982-37c-0481.pdf | | | Identifier
| ZNC-1982-37c-0481 | | | Volume
| 37 | |
7 | Author
| Ulrich Schraermeyer | Requires cookie* | | Title
| Evidence for a Pathway of Distal Screening Pigment Granules across the Basement Membrane of the Crayfish Photoreceptor  | | | Abstract
| The distal pigment cells o f Orconectes limosus contain two layers o f large electron lucent vacuoles that are separated by layers o f small right-angled platelets adjacent to the crystalline cones. The crystalline cones o f the dioptric apparatus o f this species have evaginations into the distal pigment cell cytoplasm. In photoreceptors o f Orconectes limosus and Procambarus clar-kii a dark pigment accumulation site was detected just distal to the basement membrane at the edges o f each retina. These pigment accumulations occurred independent o f the state o f light adaptation. Ultrastructurally the pigment granules at this accumulation site resemble distal screening pigment granules according to their size (up to 1.2 jim in diameter) and fibrous structure. Distal screening pigment granules were also found in tube-like cell processes or ex-tracellularly within and proximal to the retinal basement membrane, indicating pigment trans port to and across the basement membrane. Proximal to the basement membrane screening pigment granules were also observed disintegrated to a gravel-like electron dense material in widely branched cells. Evidence was found that an electron dense material, probably resulting from disintegrating screening pigment granules, was incorporated in the integument o f the eyestalk. Four hours after injection o f gold particles into the eye stalk distal to the retina they were detected inside and proximal to the retinal basement membrane. | | |
Reference
| Z. Naturforsch. 47c, 453 (1992); received June 13 1991/February 11 1992 | | |
Published
| 1992 | | |
Keywords
| Electron Microscopy, Crayfish, Distal Screening Pigment Granules, Basement Membrane, Crystalline Cone | | |
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| default:Reihe_C/47/ZNC-1992-47c-0453.pdf | | | Identifier
| ZNC-1992-47c-0453 | | | Volume
| 47 | |
9 | Author
| Marvin Stromer, Wilhelm Hasselbadh | Requires cookie* | | Title
| Fusion of Isolated Sarcoplasmic Reticulum Membranes  | | | Abstract
| Fragmented sarcoplasmic reticulum (FSR) vesicles from rabbit muscle were suspended in 1.5 — 5% glycerol solutions and were pelleted onto aluminum foil disks in a modified centrifuge tube. Examination of these pellets in the electron microscope after drying for 2 — 2.5, 4 — 5.5, and 21 hours revealed a progression of changes. First, distances between individual, round vesicles decreases. Next, somewhat flattened vesicles establish limited areas of contact with adjacent vesicles. Finally, vesicle fusion occurs and extended areas of double bilayers are formed. A water loss-time interaction appears to be needed for the fusion process. A Hg-phenyl azoferritin com pound was used as a marker to identify intra-and extra-vesicular space in the fused samples. Quantitative measurements of birefringence during imbibition of pellet slices in a graded series of glycerol solutions indicates a steadily increasing amount of birefringence until 60 — 80% glycerol (»/ = 1.41 —1.43) is readied. The plateau seen in this part of the curve is again followed by steadily increasing birefringence at higher glycerol concentrations. This interruption in the birefringence curve is presumably due to a matching of the refractive indices of the glycerol solution and a lipid component in the membranes. | | |
Reference
| (Z. Naturforsch. 31c, 703 [1976]; received August 23 1976) | | |
Published
| 1976 | | |
Keywords
| Membrane Fusion, Sarcoplasmic Reticulum, Glycerol, Electron Microscopy, Polarizing Microscopy | | |
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| default:Reihe_C/31/ZNC-1976-31c-0703.pdf | | | Identifier
| ZNC-1976-31c-0703 | | | Volume
| 31 | |
11 | Author
| Riidiger Riehl | Requires cookie* | | Title
| Parakristalline Körper in jungen Oocyten der Schmerle  | | | Abstract
| N o em a ch eilu s barbatulus (L.) (Teleostei, Cobitidae) Paracristalline Bodies in Young Oocytes of the Loach, Noemacheilus barbatulus (L.) (Teleostei, Cobitidae) Young oocytes of the loach, Noemacheilus barbatulus (L.), were studied by electron microscopy. Fistular paracristalline bodies are found in the oocytes during state I. They consist of many osmiophilic particles with a diameter of 150 — 300 A. Ultrahistochemical experiments have demonstrated that the paracristalline bodies are mainly composed of pro teins. The paracristalline bodies are yolk precursors. | | |
Reference
| (Z. Naturforsch. 32c, 305 [1977]; eingegangen am 26. Januar 1977) | | |
Published
| 1977 | | |
Keywords
| Paracristalline Bodies, Oocytes, Yolk Precursors, Electron Microscopy, Noemacheilus barbatulus | | |
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| default:Reihe_C/32/ZNC-1977-32c-0305_n.pdf | | | Identifier
| ZNC-1977-32c-0305_n | | | Volume
| 32 | |
13 | Author
| Jürgen Kreft | Requires cookie* | | Title
| Reovirus-Specific Messenger Ribonucleoprotein Particles from Heia Cells  | | | Abstract
| When reovirus-infected Heia cells are incubated at 43 °C virus-specific messenger RNA is released from the polysomes. It accumulates free in the cytoplasm as messenger ribonucleopro tein particles (mRNPs). These particles have a sedimentation rate of about 50 S and a buoyant density in CsCl of 1.42 g/cm 3. Reovirus mRNPs contain, besides all three size classes o f reovirus messenger RNA, the same spectrum of proteins found in the polysomal mRNPs from uninfected cells, plus two additional proteins with molecular masses of 70000 d and 110000 d, respectively. Electron microscopic examination of the reovirus structures with a total mean length of 0.5 nm. | | |
Reference
| Z. Naturforsch. 35c, 1046—1051 (1980); received May 14/August 13 1980 | | |
Published
| 1980 | | |
Keywords
| Heia Cells, Reovirus, Messenger Ribonucleoprotein Particles, mRNP-Proteins, Electron Microscopy | | |
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| default:Reihe_C/35/ZNC-1980-35c-1046.pdf | | | Identifier
| ZNC-1980-35c-1046 | | | Volume
| 35 | |
15 | Author
| H. Wesch, R. Jonak, H. Nemetschek-Gansler, H. Riedl, Th Nemetschek | Requires cookie* | | Title
| Der Einfluß von D-Penicillamin auf den Gehalt einiger Organe an Spurenelementen sowie auf die mechanischen Eigenschaften von Kollagen Trace Elements in Several Organs and Mechanical Properties of Collagen under the Influence of D-Penicillamin  | | | Abstract
| The content of trace elements in several organs of rats under the influence of D-penicillamine (D-PA) was investigated by the neutronactivation-analysis. It could be shown an diminution of Cu, and Co under D-PA-treatment, the content of Fe, Mn, Rb and Zn was not influenced. The investigat ed organs didn't show any submicroscopic alterations under D-PA. On isolated collagen fibrils of tail tendon was seen a significantly diminuition of E-moduls. In accordance with Siegel the principal effect of D-PA is thought to block the synthesis of functional groups from Schiff-base crosslink precursors but not to inhibit lysyloxidase by loss of Cu-ions of connective tissue. The thermostability of D-PA influenced fibrils is changed in stretched state only and will be due to the lack of crosslink Schiff-bases; where as the shrinking point of not stretched fibrils shows only aging dependent changes. | | |
Reference
| Z. Naturforsch. 33c, 346 (1978); eingegangen am 17. März 1978 | | |
Published
| 1978 | | |
Keywords
| D-Penicillamin, Trace Elements, Electron Microscopy, Biosynthesis, Cross-Links, Mechanical Properties of Collagen | | |
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| default:Reihe_C/33/ZNC-1978-33c-0346.pdf | | | Identifier
| ZNC-1978-33c-0346 | | | Volume
| 33 | |
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