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The preparation of Bi2Sea single crystals with low free carrier densities allowed an investigation of the lattice vibrations to be carried out from the reflectivity of cleavage planes at nearly normal incidence of the radiation (E ~ c). The experimental results ean be explained with two classical oscillators, whose eigenfrequencies oceur at 92 and 69.5 cm-I. The static dielectric constant was determined to be 100 ± 10 for E ~ c.
The photoconductivity of both undeformed and deformed Te samples has been investigated at liquid He temperature by means of a Fourier spectrometer. Three peaks were usually found in the spectra of undeformed samples at 11, 24 and 46 cm\(^{-1}\). These are shown to be due to three different chemical impurities. The deformed samples are characterized by additional structure at higher frequencies.
The observed impurity induced far-infrared absorption in CsCl : Rb\(^+\) and CsCl : K\(^+\) is compared with a calculated density of acoustic phonon states in CsCl. The absorption due to CsCl : Rb\(^+\) displays a minimum between the acoustic and optic phonon bands. A narrow line is observed in CsCl: K\(^+\) at 85.8 cm\(^{-1}\) which falls in this quasi-phonon gap.
Precipitating anti-PM-Sel antibodies are present in sera from patients with polymyositis. scleroderma. and polymyositis/scleroderma overlap syndromes. By indirect immunofluorescence microscopy. anti-PM-Scl antibodies stained the nucleolus in cells of different tissues and species. suggesting that the antigen is highly conserved. By electron microscopy, anti-PM-Scl antibodies reacted primarily with the granular component of the nuc1eolus. Drugs that inhibit rRNA synthesis had a marked effect on the expression of PM-Scl antigen. In actinomycin D-treated cells, immunofluorescence staining by anti-PM-Scl was signüicantly reduced with residual staining restricted to the granular regions of nuc1eoli. Treatment with 5,6-dichloro-beta-D- ribofuranosylbenzimidazole (DRB) also selectively reduced nuc1eolar staining. On a molecular level, anti-PM-Sel antibodies precipitated 11 polypeptides with molecular weights (Mr) ranging from 110,000 to 20,000. The Mr 80,000 and 20.000 polypeptides were phosphorylated. Evidence suggests that the PM-Scl antigen complex may be related to a prerlbosomal particle.
Antibodies to calf thymus histone H2B were purified by chromatography on DEAE-cellulose and injected into oocyte nuclei of Pleurodeles waltlii. As shown by indirect immunofluorescence these antibodies cross-reacted strongly with corresponding histones associated with lampbrush chromosomes. Shortly after injection the lateral loops of the chromosomes retracted into the chromomeres and by 3 h postinjection the 'lampbrush' appearance was completely lost and the chromosomes appeared in light-microscopic preparations as rod-like structures consisting of 10ngitudina11y coalesced chromomeres. In control oocytes injected with non-immune immunoglobulins or antibodies against a ubiquitous transcript-associated protein no morphological alterations of the lampbrush chromosomes could be observed. Electron microscopic spreads of chromosomes prepared at various times after injection of anti-H2B revealed a progressive loss of transcriptional complexes from the loop axes. Finally, higher-order chromatin configurations, like supranuc1eosomal globules (' superbeads ') or cable-like chromatin strands 50- 60 nm thick predominated, indicating complete transcriptional inactivation of a11 chromosomal regions. The results indicate that H2B antibodies react specifically with his tones associated with the transcribed DNA of lateral loops in their native state. The resulting antigenantibody complexes seem to inhibit progression of the R A polymerases along the template, thus causing the premature release of transcripts, a process analogous to the stripping effect of actinomycin D. The demonstration of histones associated with heavily transcribed regions, which are not compacted into nucleosomes but largely extended, supports the current concept that unfolding of nucleosomes to a110w transcription of the DNA does not involve dissociation of histones. In contrast, amplified ribosomal RNA genes are unaffected by injected HzB antibodies. This does not necessarily indicate absence of his tones from nucleolar chromatin, since we do not know whether it is accessible in vivo to antibodies or whether the histone antigenie determinants are masked by the presence of other proteins. The technique of injecting specific antibodies should be widely applicable when analysing the in vivo distribution of chromosomal components at the electron-microscopic level and when studying complex metabolie processes, like the cleavage and modification of RNA, by selective inhibition of defined enzymic steps.
Autoantibodies to components of the nucleolus are a unique serological feature of patients with scleroderma. There are autoantibodies of several specificities; one type produces a speckled pattern of nucleolar staining in immunofluorescence. In actinomycin D and 5,6-dichloro-{j-D-ribofuranosylbenzimidazoletreated Vero cells, staining was restricted to the fibrillar and not the granular regions. By double immunofluorescence, specific rabbit anti-RNA polymerase I antibodies stained the same fibrillar structures in drug-segregated nucleoli as scleroderma sera. Scleroderma sera immunoprecipitated 13 polypeptides from (35S)methionine-labeled HeLa cell extract with molecular weights ranging from 210,000 to 14,000. Similar polypeptides were precipitated by rabbit anti-RNA polymerase I antibodies, and their common identities were confirmed in immunoabsorption experiments. Microinjection of purified IgG from a patient with speckled nucleolar staining effectively inhibited ribosomal RNA transcription. Autoantibodies to RNA polymerase I were restricted to certain patients with scleroderma and were not found in other autoimmune diseases.
Vasoactive agents which elevate either cGMP or cAMP inhibit platelet activation by pathways sharing at least one component, the 46/50 kDa vasodilator-stimulated phosphoprotein (V ASP). V ASP is stoichiometrically phosphorylated by both cGMP-dependent and cAMPdependent protein kinases in intact human platelets, and its phosphorylation correlates very well with platelet inhibition caused by cGMP- and cAMP-elevating agents. Here we report that in human platelets spread on glass, V ASP is associated predominantly with the distal parts of radial micro filament bundles and with microfilaments outlining the periphery, whereas less V ASP is associated with a central microfilamentous ring. V ASP is also detectable in a variety of different cell types including fibroblasts and epithelial cells. In fibroblasts, V ASP is concentrated at focal contact areas, along microfilament bundles (stress fibres) in a punctate pattern, in the periphery of protruding lamellae, and is phosphorylated by cGMP- and cAMP-dependent protein kinases in response to appropriate stimuli. Evidence for the direct binding of V ASP to F -actin is also presented. The data demonstrate that V ASP is a novel phosphoprotein associated with actin filaments and focal contact areas, i.e. transmembrane junctions between microfilaments and the extracellular matrix.
We have investigated Cd\(_{1-x}\)Mn\(_x\)Te thin films with Mn concentrations of x=0.12, 0.18, 0.30, 0.52, and 0.70. These single crystal layers were grown by molecular beam epitaxy on [001] CdTe substrates. The real part of the refractive index, n, was determined below the band-gap Eo in the range of 0.5-2.5 eV at T=300 K. The parallel reOectivity was measured near the Brewster angle at the YAG laser wavelength of 1.064 J.Lm (hv= 1.165 eV). Combining these results with the optical pathlength results (nd) of reOection measurements in a Fourier spectrometer we have determined n(x,v) over a wide spectral range by utilizing a three parameter fit. The accuracy of these results for n should improve waveguide designs based on this material.
Nuclei assembled in Xenopus egg extract from purified DNA or chromatin resemble their natural counterparts in a number of structural and functional features. However, the most obvious structural element of normal interphase nuclei, the nucleolus, is absent from the in vitro reconstituted nuclei. By EM, cytological silver staining, and immunofluorescence microscopy employing antibodies directed against various nucleolar components we show that nuclei assembled in vitro contain numerous distinct aggregates that resemble prenucleolar bodies (PNBs) by several criteria. Formation of these PNB-like structures requires pore complex-mediated nuclear transport of proteins but is independent of the genetic content of the in vitro nuclei as well as transcriptional and translational events. Our data indicate that nuclei assembled in vitro are capable of initiating early steps of nucleologenesis but that the resulting PNBs are unable to fuse with each other, probably due to the absence of a functional nucleolus organizer. With appropriate modifications, this experimental system should be useful to define and analyze conditions promoting the site-specific assembly of PNBs into a coherent nucleolar body.