The glycoprotein nature of A"1 adenosine receptors
A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase t...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1986 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 140(1986), 1, Seite 406-413 |
| Übergeordnetes Werk: |
volume:140 ; year:1986 ; number:1 ; pages:406-413 |
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| 520 | |a A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase treatment alters the electrophoretic mobility of the receptor band indicating the presence of terminal neuraminic acids. Neuraminidase digestion does not influence the binding characteristics of the receptor. The totally deglycosylated receptor protein obtained by chemical treatment has an apparent molecular weight of 32,000. | ||
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(DE-627)NLEJ184183715 (DE-599)GBVNLZ184183715 DE-627 ger DE-627 rakwb eng The glycoprotein nature of A"1 adenosine receptors 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase treatment alters the electrophoretic mobility of the receptor band indicating the presence of terminal neuraminic acids. Neuraminidase digestion does not influence the binding characteristics of the receptor. The totally deglycosylated receptor protein obtained by chemical treatment has an apparent molecular weight of 32,000. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Klotz, K.-N. oth Lohse, M.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 140(1986), 1, Seite 406-413 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:140 year:1986 number:1 pages:406-413 http://dx.doi.org/10.1016/0006-291X(86)91105-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 140 1986 1 406-413 |
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(DE-627)NLEJ184183715 (DE-599)GBVNLZ184183715 DE-627 ger DE-627 rakwb eng The glycoprotein nature of A"1 adenosine receptors 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase treatment alters the electrophoretic mobility of the receptor band indicating the presence of terminal neuraminic acids. Neuraminidase digestion does not influence the binding characteristics of the receptor. The totally deglycosylated receptor protein obtained by chemical treatment has an apparent molecular weight of 32,000. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Klotz, K.-N. oth Lohse, M.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 140(1986), 1, Seite 406-413 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:140 year:1986 number:1 pages:406-413 http://dx.doi.org/10.1016/0006-291X(86)91105-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 140 1986 1 406-413 |
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(DE-627)NLEJ184183715 (DE-599)GBVNLZ184183715 DE-627 ger DE-627 rakwb eng The glycoprotein nature of A"1 adenosine receptors 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase treatment alters the electrophoretic mobility of the receptor band indicating the presence of terminal neuraminic acids. Neuraminidase digestion does not influence the binding characteristics of the receptor. The totally deglycosylated receptor protein obtained by chemical treatment has an apparent molecular weight of 32,000. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Klotz, K.-N. oth Lohse, M.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 140(1986), 1, Seite 406-413 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:140 year:1986 number:1 pages:406-413 http://dx.doi.org/10.1016/0006-291X(86)91105-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 140 1986 1 406-413 |
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(DE-627)NLEJ184183715 (DE-599)GBVNLZ184183715 DE-627 ger DE-627 rakwb eng The glycoprotein nature of A"1 adenosine receptors 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase treatment alters the electrophoretic mobility of the receptor band indicating the presence of terminal neuraminic acids. Neuraminidase digestion does not influence the binding characteristics of the receptor. The totally deglycosylated receptor protein obtained by chemical treatment has an apparent molecular weight of 32,000. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Klotz, K.-N. oth Lohse, M.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 140(1986), 1, Seite 406-413 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:140 year:1986 number:1 pages:406-413 http://dx.doi.org/10.1016/0006-291X(86)91105-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 140 1986 1 406-413 |
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The glycoprotein nature of A"1 adenosine receptors |
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A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase treatment alters the electrophoretic mobility of the receptor band indicating the presence of terminal neuraminic acids. Neuraminidase digestion does not influence the binding characteristics of the receptor. The totally deglycosylated receptor protein obtained by chemical treatment has an apparent molecular weight of 32,000. |
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A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase treatment alters the electrophoretic mobility of the receptor band indicating the presence of terminal neuraminic acids. Neuraminidase digestion does not influence the binding characteristics of the receptor. The totally deglycosylated receptor protein obtained by chemical treatment has an apparent molecular weight of 32,000. |
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A"1 adenosine receptors from different tissues and species were photoaffinity labelled and then the carbohydrate content was examined by both enzymatic and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the labelled membrane receptors shows that neuraminidase treatment alters the electrophoretic mobility of the receptor band indicating the presence of terminal neuraminic acids. Neuraminidase digestion does not influence the binding characteristics of the receptor. The totally deglycosylated receptor protein obtained by chemical treatment has an apparent molecular weight of 32,000. |
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