GTP analogues cause release of the alpha subunit of the GTP binding protein, G"O, from the plasma membrane of NG108-15 cells
Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiment...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1988 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 152(1988), 1, Seite 243-251 |
| Übergeordnetes Werk: |
volume:152 ; year:1988 ; number:1 ; pages:243-251 |
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| 520 | |a Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment. | ||
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(DE-627)NLEJ176985220 (DE-599)GBVNLZ176985220 DE-627 ger DE-627 rakwb eng GTP analogues cause release of the alpha subunit of the GTP binding protein, G"O, from the plasma membrane of NG108-15 cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 McArdle, H. oth Mullaney, I. oth Magee, A. oth Unson, C. oth Milligan, G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 152(1988), 1, Seite 243-251 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:152 year:1988 number:1 pages:243-251 http://dx.doi.org/10.1016/S0006-291X(88)80706-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 152 1988 1 243-251 |
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(DE-627)NLEJ176985220 (DE-599)GBVNLZ176985220 DE-627 ger DE-627 rakwb eng GTP analogues cause release of the alpha subunit of the GTP binding protein, G"O, from the plasma membrane of NG108-15 cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 McArdle, H. oth Mullaney, I. oth Magee, A. oth Unson, C. oth Milligan, G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 152(1988), 1, Seite 243-251 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:152 year:1988 number:1 pages:243-251 http://dx.doi.org/10.1016/S0006-291X(88)80706-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 152 1988 1 243-251 |
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(DE-627)NLEJ176985220 (DE-599)GBVNLZ176985220 DE-627 ger DE-627 rakwb eng GTP analogues cause release of the alpha subunit of the GTP binding protein, G"O, from the plasma membrane of NG108-15 cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 McArdle, H. oth Mullaney, I. oth Magee, A. oth Unson, C. oth Milligan, G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 152(1988), 1, Seite 243-251 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:152 year:1988 number:1 pages:243-251 http://dx.doi.org/10.1016/S0006-291X(88)80706-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 152 1988 1 243-251 |
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(DE-627)NLEJ176985220 (DE-599)GBVNLZ176985220 DE-627 ger DE-627 rakwb eng GTP analogues cause release of the alpha subunit of the GTP binding protein, G"O, from the plasma membrane of NG108-15 cells 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 McArdle, H. oth Mullaney, I. oth Magee, A. oth Unson, C. oth Milligan, G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 152(1988), 1, Seite 243-251 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:152 year:1988 number:1 pages:243-251 http://dx.doi.org/10.1016/S0006-291X(88)80706-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 152 1988 1 243-251 |
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gtp analogues cause release of the alpha subunit of the gtp binding protein, g"o, from the plasma membrane of ng108-15 cells |
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GTP analogues cause release of the alpha subunit of the GTP binding protein, G"O, from the plasma membrane of NG108-15 cells |
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Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment. |
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Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment. |
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Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment. |
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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">NLEJ176985220</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706035435.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070505s1988 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ176985220</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ176985220</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">GTP analogues cause release of the alpha subunit of the GTP binding protein, G"O, from the plasma membrane of NG108-15 cells</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1988</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">Incubation of membranes of neuroblastoma x glioma hybrid, NG108-15 cells with GDPβS followed by immunoblotting of resolved membrane and supernatant fractions with specific anti-peptide antisera showed essentially all of the α subunit of G"O to be associated with the membrane. Similar experiments with poorly hydrolyzed analogues of GTP caused release of a significant fraction (some 50% within 60 minutes) of G"Oα into the supernatant. This was not mimicked by analogues of ATP. Antisera directed against peptides corresponding to the extreme N and C-termini of G"Oα demonstrated that the released polypeptide was not proteolytically clipped. These experiments show that the α subunit of G"O need not be invariably bound to the plasma membrane and that guanine nucleotide activation can release the alpha subunit of G"O from its site of membrane attachment.</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">McArdle, H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mullaney, I.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Magee, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Unson, C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Milligan, G.</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">152(1988), 1, Seite 243-251</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:152</subfield><subfield code="g">year:1988</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:243-251</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/S0006-291X(88)80706-X</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">152</subfield><subfield code="j">1988</subfield><subfield code="e">1</subfield><subfield code="h">243-251</subfield></datafield></record></collection>
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7.399288 |