Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium
When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, t...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1985 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Biomembranes - Amsterdam : Elsevier, 813(1985), 1, Seite 111-116 |
| Übergeordnetes Werk: |
volume:813 ; year:1985 ; number:1 ; pages:111-116 |
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NLEJ185842828 |
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| 245 | 1 | 0 | |a Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium |
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| 520 | |a When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. | ||
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(DE-627)NLEJ185842828 (DE-599)GBVNLZ185842828 DE-627 ger DE-627 rakwb eng Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hyono, A. oth Kuriyama, S. oth Masui, M. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 813(1985), 1, Seite 111-116 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:813 year:1985 number:1 pages:111-116 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(85)90351-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 813 1985 1 111-116 |
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(DE-627)NLEJ185842828 (DE-599)GBVNLZ185842828 DE-627 ger DE-627 rakwb eng Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hyono, A. oth Kuriyama, S. oth Masui, M. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 813(1985), 1, Seite 111-116 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:813 year:1985 number:1 pages:111-116 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(85)90351-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 813 1985 1 111-116 |
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(DE-627)NLEJ185842828 (DE-599)GBVNLZ185842828 DE-627 ger DE-627 rakwb eng Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hyono, A. oth Kuriyama, S. oth Masui, M. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 813(1985), 1, Seite 111-116 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:813 year:1985 number:1 pages:111-116 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(85)90351-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 813 1985 1 111-116 |
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(DE-627)NLEJ185842828 (DE-599)GBVNLZ185842828 DE-627 ger DE-627 rakwb eng Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hyono, A. oth Kuriyama, S. oth Masui, M. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 813(1985), 1, Seite 111-116 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:813 year:1985 number:1 pages:111-116 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(85)90351-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 813 1985 1 111-116 |
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(DE-627)NLEJ185842828 (DE-599)GBVNLZ185842828 DE-627 ger DE-627 rakwb eng Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hyono, A. oth Kuriyama, S. oth Masui, M. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 813(1985), 1, Seite 111-116 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:813 year:1985 number:1 pages:111-116 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(85)90351-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 813 1985 1 111-116 |
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fluorescence energy transfer between ionophore, a23187, and membrane proteins of isolated outer and cytoplasmic membranes of a gram-negative bacterium |
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Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium |
| abstract |
When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. |
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When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. |
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When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ185842828</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707030313.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1985 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185842828</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185842828</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Fluorescence energy transfer between ionophore, A23187, and membrane proteins of isolated outer and cytoplasmic membranes of a Gram-negative bacterium</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1985</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">When trytophan residues of the proteins of outer and cytoplasmic membranes of a modeprately halophilic bacterium, Pseudomanas halosaccharolytica ATCC 29423, were excited at the wavelength 270 nm, tryptophan emission was observed at 330 nm. Adding the calcium ionophore, A23187, to both suspensions, the tryptophan emission at 330 nm decreased and the ionophore emission at 430 nm increased. Thus, when the calcium ionophore was increased in both suspensions, the ionophore emission increased with excitation of membrane tryptophan, that is, the fluorescence energy was transferred from tryptophan to the calcium ionophore. Using the Forster equation the critical distance was calculated to be 52 Å. As this distance is considerable compared with the diameter of the membrane protein molecules, the ionophore cannot be bound to the membrane proteins. It is probably located in the lipid bilayers.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hyono, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kuriyama, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Masui, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/Biomembranes</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">813(1985), 1, Seite 111-116</subfield><subfield code="w">(DE-627)NLEJ185706983</subfield><subfield code="w">(DE-600)2209384-9</subfield><subfield code="x">0005-2736</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:813</subfield><subfield code="g">year:1985</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:111-116</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0005-2736(85)90351-7</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">813</subfield><subfield code="j">1985</subfield><subfield code="e">1</subfield><subfield code="h">111-116</subfield></datafield></record></collection>
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