Absorption spectra of viral components of Sendai virus in the wavelength region from 130 to 320 nm
Identifieur interne : 001017 ( Istex/Curation ); précédent : 001016; suivant : 001018Absorption spectra of viral components of Sendai virus in the wavelength region from 130 to 320 nm
Auteurs : Tsuneo Megumi [Japon] ; Ryosuke Nishikawa [Japon] ; Shinich Fujita [Japon] ; Mikio Saito [Japon] ; Takashi Ito [Japon]Source :
- Journal of Photochemistry & Photobiology, B: Biology [ 1011-1344 ] ; 1991.
English descriptors
- Teeft :
- Absorption, Absorption coefficient, Absorption measurements, Absorption spectra, Absorption spectrum, Allantoic fluid, Apparent mass absorption, Apparent mass absorption coefficient, Broad peak, Cafa plate, Cell membrane, Coefficient, Core proteins, Diffuse reflection, Double bonds, Envelope particles, Fatty acids, Good agreement, Large increase, Light loss, Light source, Lipid, Lipid bilayers, Mass absorption coefficient, Mass absorption coefficients, Molecular weight, Nucleic, Nucleic acids, Optical properties, Osaka prefecture, Reconstructed envelopes, Sample film, Sample weights, Sendai, Sendai virus, Sharp increase, Slight peak, Spike, Spike glycoproteins, Spike proteins, Subunit, Synchrotron, Synchrotron radiation, Thii films, Thin films, Viral, Viral components, Virion, Wavelength range, Wavelength region, Whole virion, Whole virions.
Abstract
Abstract: Using synchrotron radiation as a light source, the absorption spectra of purified viral components of the Sendai virus, i.e. messenger RNA, lipids, spike (envelope) proteins, reconstructed envelopes, core proteins and whole virions, were obtained in the wavelength region 130–320 nm by measuring the transmission of thin films. Viral (messenger) RNA two peaks at 260 and 190 nm, and a large increase below 160 nm. The absorption spectrum of lipids exhibited a broad peak at 190 nm and a very sharp increase below 160 nm. With spike proteins, a slight peak at 280 nm and a shoulder at 230 nm were observed in addition to a sharper peak at 190 nm and a rather slow increasing absorption below 160 nm. Reconstructed envelopes showed the features of a combination of lipids and proteins. The absorption spectra of core proteins and whole virions exhibited similar characteristics to spike proteins. Conventional UV data were also obtained in the wavelength range 210–320 nm with RNA and lipids. The UV and synchrotron radiation data were in good agreement in terms of the mass absorption coefficients. The molecular splitting of spike proteins was also examined. Proteins gave more diffuse reflection than their subunits, causing a reduction in absorption. This was explained by a loss of transparency with increasing molecular weight.
Url:
DOI: 10.1016/1011-1344(91)80214-3
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xml:lang="fr">Japon</country><wicri:regionArea>Research Institute for Science and Technology, University of Osaka Prefecture, Sakai</wicri:regionArea></affiliation></author><author><name sortKey="Fujita, Shinich" sort="Fujita, Shinich" uniqKey="Fujita S" first="Shinich" last="Fujita">Shinich Fujita</name><affiliation wicri:level="1"><mods:affiliation>Research Institute for Science and Technology, University of Osaka Prefecture, Sakai, Osaka 593 Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Research Institute for Science and Technology, University of Osaka Prefecture, Sakai</wicri:regionArea></affiliation></author><author><name sortKey="Saito, Mikio" sort="Saito, Mikio" uniqKey="Saito M" first="Mikio" last="Saito">Mikio Saito</name><affiliation wicri:level="1"><mods:affiliation>Biophysical Laboratory, Rikkyo University, Nishiikebukuro, Toshima-ku, Tokyo 171 Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Biophysical Laboratory, Rikkyo University, Nishiikebukuro, Toshima-ku</wicri:regionArea></affiliation></author><author><name sortKey="Ito, Takashi" sort="Ito, Takashi" uniqKey="Ito T" first="Takashi" last="Ito">Takashi Ito</name><affiliation wicri:level="1"><mods:affiliation>Institute of Physics, College of Arts and Sciences, University of Tokyo, Komaba, Meguro-ku, Tokyo 153 Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Institute of Physics, College of Arts and Sciences, University of Tokyo, Komaba, Meguro-ku</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:7668972446A7FB40264D01F85B338093598EFE85</idno><date when="1991" year="1991">1991</date><idno type="doi">10.1016/1011-1344(91)80214-3</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-W2CGNJ13-N/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001017</idno><idno type="wicri:explorRef" wicri:stream="Istex" 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University of Osaka Prefecture, Sakai, Osaka 593 Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Research Institute for Science and Technology, University of Osaka Prefecture, Sakai</wicri:regionArea></affiliation></author><author><name sortKey="Fujita, Shinich" sort="Fujita, Shinich" uniqKey="Fujita S" first="Shinich" last="Fujita">Shinich Fujita</name><affiliation wicri:level="1"><mods:affiliation>Research Institute for Science and Technology, University of Osaka Prefecture, Sakai, Osaka 593 Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Research Institute for Science and Technology, University of Osaka Prefecture, Sakai</wicri:regionArea></affiliation></author><author><name sortKey="Saito, Mikio" sort="Saito, Mikio" uniqKey="Saito M" first="Mikio" last="Saito">Mikio Saito</name><affiliation wicri:level="1"><mods:affiliation>Biophysical Laboratory, Rikkyo University, Nishiikebukuro, Toshima-ku, Tokyo 171 Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Biophysical Laboratory, Rikkyo University, Nishiikebukuro, Toshima-ku</wicri:regionArea></affiliation></author><author><name sortKey="Ito, Takashi" sort="Ito, Takashi" uniqKey="Ito T" first="Takashi" last="Ito">Takashi Ito</name><affiliation wicri:level="1"><mods:affiliation>Institute of Physics, College of Arts and Sciences, University of Tokyo, Komaba, Meguro-ku, Tokyo 153 Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Institute of Physics, College of Arts and Sciences, University of Tokyo, Komaba, Meguro-ku</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Photochemistry & Photobiology, B: Biology</title><title level="j" type="abbrev">JPB</title><idno type="ISSN">1011-1344</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">10</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="79">79</biblScope><biblScope unit="page" to="89">89</biblScope></imprint><idno type="ISSN">1011-1344</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1011-1344</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Absorption</term><term>Absorption coefficient</term><term>Absorption measurements</term><term>Absorption spectra</term><term>Absorption spectrum</term><term>Allantoic fluid</term><term>Apparent mass absorption</term><term>Apparent mass absorption coefficient</term><term>Broad peak</term><term>Cafa plate</term><term>Cell membrane</term><term>Coefficient</term><term>Core proteins</term><term>Diffuse reflection</term><term>Double bonds</term><term>Envelope particles</term><term>Fatty acids</term><term>Good agreement</term><term>Large increase</term><term>Light loss</term><term>Light source</term><term>Lipid</term><term>Lipid bilayers</term><term>Mass absorption coefficient</term><term>Mass absorption coefficients</term><term>Molecular weight</term><term>Nucleic</term><term>Nucleic acids</term><term>Optical properties</term><term>Osaka prefecture</term><term>Reconstructed envelopes</term><term>Sample film</term><term>Sample weights</term><term>Sendai</term><term>Sendai virus</term><term>Sharp increase</term><term>Slight peak</term><term>Spike</term><term>Spike glycoproteins</term><term>Spike proteins</term><term>Subunit</term><term>Synchrotron</term><term>Synchrotron radiation</term><term>Thii films</term><term>Thin films</term><term>Viral</term><term>Viral components</term><term>Virion</term><term>Wavelength range</term><term>Wavelength region</term><term>Whole virion</term><term>Whole virions</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Using synchrotron radiation as a light source, the absorption spectra of purified viral components of the Sendai virus, i.e. messenger RNA, lipids, spike (envelope) proteins, reconstructed envelopes, core proteins and whole virions, were obtained in the wavelength region 130–320 nm by measuring the transmission of thin films. Viral (messenger) RNA two peaks at 260 and 190 nm, and a large increase below 160 nm. The absorption spectrum of lipids exhibited a broad peak at 190 nm and a very sharp increase below 160 nm. With spike proteins, a slight peak at 280 nm and a shoulder at 230 nm were observed in addition to a sharper peak at 190 nm and a rather slow increasing absorption below 160 nm. Reconstructed envelopes showed the features of a combination of lipids and proteins. The absorption spectra of core proteins and whole virions exhibited similar characteristics to spike proteins. Conventional UV data were also obtained in the wavelength range 210–320 nm with RNA and lipids. The UV and synchrotron radiation data were in good agreement in terms of the mass absorption coefficients. The molecular splitting of spike proteins was also examined. Proteins gave more diffuse reflection than their subunits, causing a reduction in absorption. This was explained by a loss of transparency with increasing molecular weight.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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