Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction
The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1977 |
|---|
| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 78(1977), 2, Seite 525-533 |
| Übergeordnetes Werk: |
volume:78 ; year:1977 ; number:2 ; pages:525-533 |
| Links: |
|---|
| Katalog-ID: |
NLEJ184214521 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ184214521 | ||
| 003 | DE-627 | ||
| 005 | 20210706223908.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 070506s1977 xx |||||o 00| ||eng c | ||
| 035 | |a (DE-627)NLEJ184214521 | ||
| 035 | |a (DE-599)GBVNLZ184214521 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 245 | 1 | 0 | |a Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction |
| 264 | 1 | |c 1977 | |
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. | ||
| 533 | |f Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 | ||
| 700 | 1 | |a Mihovilovic, M. |4 oth | |
| 700 | 1 | |a Nowak, T. |4 oth | |
| 700 | 1 | |a Raftery, M.A. |4 oth | |
| 700 | 1 | |a Martinez-Carrion, M. |4 oth | |
| 773 | 0 | 8 | |i in |t Biochemical and Biophysical Research Communications |d Amsterdam : Elsevier |g 78(1977), 2, Seite 525-533 |w (DE-627)NLEJ176855645 |w (DE-600)1461396-7 |x 0006-291X |7 nnns |
| 773 | 1 | 8 | |g volume:78 |g year:1977 |g number:2 |g pages:525-533 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1016/0006-291X(77)90210-8 |
| 912 | |a GBV_USEFLAG_H | ||
| 912 | |a ZDB-1-SDJ | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 78 |j 1977 |e 2 |h 525-533 | ||
| matchkey_str |
article:0006291X:1977----::idnsuisfntioaeaeycoieeetrspoeoc |
|---|---|
| hierarchy_sort_str |
1977 |
| publishDate |
1977 |
| allfields |
(DE-627)NLEJ184214521 (DE-599)GBVNLZ184214521 DE-627 ger DE-627 rakwb eng Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mihovilovic, M. oth Nowak, T. oth Raftery, M.A. oth Martinez-Carrion, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 78(1977), 2, Seite 525-533 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:78 year:1977 number:2 pages:525-533 http://dx.doi.org/10.1016/0006-291X(77)90210-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 78 1977 2 525-533 |
| spelling |
(DE-627)NLEJ184214521 (DE-599)GBVNLZ184214521 DE-627 ger DE-627 rakwb eng Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mihovilovic, M. oth Nowak, T. oth Raftery, M.A. oth Martinez-Carrion, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 78(1977), 2, Seite 525-533 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:78 year:1977 number:2 pages:525-533 http://dx.doi.org/10.1016/0006-291X(77)90210-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 78 1977 2 525-533 |
| allfields_unstemmed |
(DE-627)NLEJ184214521 (DE-599)GBVNLZ184214521 DE-627 ger DE-627 rakwb eng Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mihovilovic, M. oth Nowak, T. oth Raftery, M.A. oth Martinez-Carrion, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 78(1977), 2, Seite 525-533 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:78 year:1977 number:2 pages:525-533 http://dx.doi.org/10.1016/0006-291X(77)90210-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 78 1977 2 525-533 |
| allfieldsGer |
(DE-627)NLEJ184214521 (DE-599)GBVNLZ184214521 DE-627 ger DE-627 rakwb eng Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mihovilovic, M. oth Nowak, T. oth Raftery, M.A. oth Martinez-Carrion, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 78(1977), 2, Seite 525-533 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:78 year:1977 number:2 pages:525-533 http://dx.doi.org/10.1016/0006-291X(77)90210-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 78 1977 2 525-533 |
| allfieldsSound |
(DE-627)NLEJ184214521 (DE-599)GBVNLZ184214521 DE-627 ger DE-627 rakwb eng Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mihovilovic, M. oth Nowak, T. oth Raftery, M.A. oth Martinez-Carrion, M. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 78(1977), 2, Seite 525-533 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:78 year:1977 number:2 pages:525-533 http://dx.doi.org/10.1016/0006-291X(77)90210-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 78 1977 2 525-533 |
| language |
English |
| source |
in Biochemical and Biophysical Research Communications 78(1977), 2, Seite 525-533 volume:78 year:1977 number:2 pages:525-533 |
| sourceStr |
in Biochemical and Biophysical Research Communications 78(1977), 2, Seite 525-533 volume:78 year:1977 number:2 pages:525-533 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Biochemical and Biophysical Research Communications |
| authorswithroles_txt_mv |
Mihovilovic, M. @@oth@@ Nowak, T. @@oth@@ Raftery, M.A. @@oth@@ Martinez-Carrion, M. @@oth@@ |
| publishDateDaySort_date |
1977-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ176855645 |
| id |
NLEJ184214521 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ184214521</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706223908.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1977 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ184214521</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ184214521</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">Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1977</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">The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2.</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">Mihovilovic, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Nowak, T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Raftery, M.A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Martinez-Carrion, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochemical and Biophysical Research Communications</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">78(1977), 2, Seite 525-533</subfield><subfield code="w">(DE-627)NLEJ176855645</subfield><subfield code="w">(DE-600)1461396-7</subfield><subfield code="x">0006-291X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:78</subfield><subfield code="g">year:1977</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:525-533</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0006-291X(77)90210-8</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">78</subfield><subfield code="j">1977</subfield><subfield code="e">2</subfield><subfield code="h">525-533</subfield></datafield></record></collection>
|
| series2 |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ176855645 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| collection |
NL |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
0006-291X |
| topic_title |
Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
m m mm t n tn m r mr m m c mmc |
| hierarchy_parent_title |
Biochemical and Biophysical Research Communications |
| hierarchy_parent_id |
NLEJ176855645 |
| hierarchy_top_title |
Biochemical and Biophysical Research Communications |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ176855645 (DE-600)1461396-7 |
| title |
Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction |
| spellingShingle |
Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction |
| ctrlnum |
(DE-627)NLEJ184214521 (DE-599)GBVNLZ184214521 |
| title_full |
Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction |
| journal |
Biochemical and Biophysical Research Communications |
| journalStr |
Biochemical and Biophysical Research Communications |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1977 |
| contenttype_str_mv |
zzz |
| container_start_page |
525 |
| container_volume |
78 |
| format_se |
Elektronische Aufsätze |
| title_sort |
binding studies of mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction |
| title_auth |
Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction |
| abstract |
The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. |
| abstractGer |
The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. |
| abstract_unstemmed |
The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2. |
| collection_details |
GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE |
| container_issue |
2 |
| title_short |
Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction |
| url |
http://dx.doi.org/10.1016/0006-291X(77)90210-8 |
| remote_bool |
true |
| author2 |
Mihovilovic, M. Nowak, T. Raftery, M.A. Martinez-Carrion, M. |
| author2Str |
Mihovilovic, M. Nowak, T. Raftery, M.A. Martinez-Carrion, M. |
| ppnlink |
NLEJ176855645 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth oth |
| up_date |
2024-07-06T00:33:54.500Z |
| _version_ |
1803787734353969152 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ184214521</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706223908.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1977 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ184214521</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ184214521</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">Binding studies of Mn^+^2 to isolated acetylcholine receptor as a probe for cation-receptor interaction</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1977</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">The paramagnetic cation Mn^+^2 binds to Torpedo californica acetylcholine receptor (AcChR) at sites with at least two different affinity constants. For each α-Bungarotoxin (α-Bgt) binding site AcChR has between 3 to 4 Mn^+^2 sites with Kd values of 1.74 +/- 1.0 x 10^-^4 M. An additional 10-12 sites/α-Bgt site have a weaker affinity for Mn^+^2 (Kd 1 mM). The α-Bgt does not displace bound Mn^+^2, however Ca^+^2 displaces all bound Mn^+^2 in a competitive fashion with Kd of 0.90 x 10^-^3 M and Mg^+^2 is as effective as Ca^+^2 in the displacement. Decamethonium, carbamylcholine and NaCl at high concentrations are also effective in displacing Mn^+^2. A constant enhancement value (ε"b) for the binary metal . AcChR complexes was obtained when simultaneous EPR measurements and the water proton relaxation rates were made. Similarity of the AcChR environment and/or coordination number for the Mn^+^2 sites in AcChR is inferred. It appears that Mn^+^2 binds to many AcChR sites, different from those responsible for binding cholinergic ligands. The Mn^+^2 site seem to be the same as those responsible for binding the electrophysiologically significant Ca^+^2.</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">Mihovilovic, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Nowak, T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Raftery, M.A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Martinez-Carrion, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochemical and Biophysical Research Communications</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">78(1977), 2, Seite 525-533</subfield><subfield code="w">(DE-627)NLEJ176855645</subfield><subfield code="w">(DE-600)1461396-7</subfield><subfield code="x">0006-291X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:78</subfield><subfield code="g">year:1977</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:525-533</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0006-291X(77)90210-8</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">78</subfield><subfield code="j">1977</subfield><subfield code="e">2</subfield><subfield code="h">525-533</subfield></datafield></record></collection>
|
| score |
7.3979874 |