A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa
Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1988 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 155(1988), 1, Seite 59-65 |
| Übergeordnetes Werk: |
volume:155 ; year:1988 ; number:1 ; pages:59-65 |
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| 245 | 1 | 2 | |a A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa |
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| 520 | |a Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. | ||
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(DE-627)NLEJ184957036 (DE-599)GBVNLZ184957036 DE-627 ger DE-627 rakwb eng A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Fawell, S.E. oth Lenard, J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 155(1988), 1, Seite 59-65 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:155 year:1988 number:1 pages:59-65 http://dx.doi.org/10.1016/S0006-291X(88)81049-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 155 1988 1 59-65 |
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(DE-627)NLEJ184957036 (DE-599)GBVNLZ184957036 DE-627 ger DE-627 rakwb eng A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Fawell, S.E. oth Lenard, J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 155(1988), 1, Seite 59-65 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:155 year:1988 number:1 pages:59-65 http://dx.doi.org/10.1016/S0006-291X(88)81049-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 155 1988 1 59-65 |
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(DE-627)NLEJ184957036 (DE-599)GBVNLZ184957036 DE-627 ger DE-627 rakwb eng A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Fawell, S.E. oth Lenard, J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 155(1988), 1, Seite 59-65 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:155 year:1988 number:1 pages:59-65 http://dx.doi.org/10.1016/S0006-291X(88)81049-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 155 1988 1 59-65 |
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(DE-627)NLEJ184957036 (DE-599)GBVNLZ184957036 DE-627 ger DE-627 rakwb eng A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Fawell, S.E. oth Lenard, J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 155(1988), 1, Seite 59-65 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:155 year:1988 number:1 pages:59-65 http://dx.doi.org/10.1016/S0006-291X(88)81049-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 155 1988 1 59-65 |
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(DE-627)NLEJ184957036 (DE-599)GBVNLZ184957036 DE-627 ger DE-627 rakwb eng A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa 1988 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Fawell, S.E. oth Lenard, J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 155(1988), 1, Seite 59-65 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:155 year:1988 number:1 pages:59-65 http://dx.doi.org/10.1016/S0006-291X(88)81049-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 155 1988 1 59-65 |
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specific insulin receptor and tyrosine kinase activity in the membranes of neurospora crassa |
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A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa |
| abstract |
Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. |
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Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. |
| abstract_unstemmed |
Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate. |
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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">NLEJ184957036</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707003626.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1988 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ184957036</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ184957036</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="2"><subfield code="a">A specific insulin receptor and tyrosine kinase activity in the membranes of Neurospora crassa</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">Cells of the wall-less (''slime'') strain of Neurospora crassa possess specific high affinity insulin binding sites on their cell surface. ^1^2^5I-labeled bound insulin was not displaced from these cells by insulin-like growth factor II (IGF-II), and was only weakly displaced by IGF-I and proinsulin. Cross-linking of ^1^2^5I-labeled insulin with N. crassa cells using disuccinimidyl suberate resulted in the labeling of a single band of ca. 67 kDa m.w. on a polyacrylamide gel. Two proteins of ca. 66 and 59 kDa m.w. were purified from detergent solubilized plasma membrane preparations by passage over an insulin-agarose affinity matrix. Antibodies against an autophosphorylation site on the human and Drosophila insulin receptors (anti P2) immunoprecipitated a single phosphoprotein of ca. 50 kDa m.w. from detergent solubilized plasma membranes, which possessed protein tyrosine kinase activity when histone H2 was used as substrate.</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">Fawell, S.E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lenard, J.</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">155(1988), 1, Seite 59-65</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:155</subfield><subfield code="g">year:1988</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:59-65</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/S0006-291X(88)81049-0</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">155</subfield><subfield code="j">1988</subfield><subfield code="e">1</subfield><subfield code="h">59-65</subfield></datafield></record></collection>
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