Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin
Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitivel...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Muniz, Zilda M. [verfasserIn] Diniz, Carlos R. [verfasserIn] Dolly, J. Oliver [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1990 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 54(1990), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:54 ; year:1990 ; number:1 ; pages:0 |
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| DOI / URN: |
10.1111/j.1471-4159.1990.tb13320.x |
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| 520 | |a Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. | ||
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10.1111/j.1471-4159.1990.tb13320.x doi (DE-627)NLEJ240272129 DE-627 ger DE-627 rakwb Muniz, Zilda M. verfasserin aut Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Dendrotoxins Diniz, Carlos R. verfasserin aut Dolly, J. Oliver verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb13320.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 1 0 |
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10.1111/j.1471-4159.1990.tb13320.x doi (DE-627)NLEJ240272129 DE-627 ger DE-627 rakwb Muniz, Zilda M. verfasserin aut Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Dendrotoxins Diniz, Carlos R. verfasserin aut Dolly, J. Oliver verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb13320.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 1 0 |
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10.1111/j.1471-4159.1990.tb13320.x doi (DE-627)NLEJ240272129 DE-627 ger DE-627 rakwb Muniz, Zilda M. verfasserin aut Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Dendrotoxins Diniz, Carlos R. verfasserin aut Dolly, J. Oliver verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb13320.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 1 0 |
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10.1111/j.1471-4159.1990.tb13320.x doi (DE-627)NLEJ240272129 DE-627 ger DE-627 rakwb Muniz, Zilda M. verfasserin aut Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Dendrotoxins Diniz, Carlos R. verfasserin aut Dolly, J. Oliver verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb13320.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 1 0 |
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10.1111/j.1471-4159.1990.tb13320.x doi (DE-627)NLEJ240272129 DE-627 ger DE-627 rakwb Muniz, Zilda M. verfasserin aut Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Dendrotoxins Diniz, Carlos R. verfasserin aut Dolly, J. Oliver verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb13320.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 1 0 |
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Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin Dendrotoxins |
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Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin |
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Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. |
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Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. |
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Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. It is concluded that δ-dendrotoxin interacts with a distinct site on the oligomeric acceptors for α-dendrotoxin. |
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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">NLEJ240272129</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707105430.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1990 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1471-4159.1990.tb13320.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240272129</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="100" ind1="1" ind2=" "><subfield code="a">Muniz, Zilda M.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Characterisation of Binding Sites for δ-Dendrotoxin in Guinea-Pig Synaptosomes: Relationship to Acceptors for the K+-Channel Probe α-Dendrotoxin</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1990</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</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">Abstract: With use of biologically active 125I-labelled δ-dendrotoxin, a putative K+-channel ligand, homogeneous, noninteracting, high-affinity acceptors (KD= 0.32 ± 0.07 nM; Bmax= 0.33 ± 0.04 pmol/mg) were observed in synaptosomes from guinea-pig cortex. This binding was antagonised noncompetitively by α-dendrotoxin, an inhibitor of certain fast-activating, voltage-gated K+ channels. Chemical cross-linking of the δ-dendrotoxin-acceptor complex in synaptosomes yielded two specifically labeled polypeptides with molecular masses of 69 and 82 kilodaltons. Although α-dendrotoxin prevents the labelling of both these bands, it cross-linked only a single protein with a molecular mass of 69 kilodaltons. 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7.401025 |