Purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells
The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities....
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1993 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: FEBS Letters - Amsterdam : Elsevier, 324(1993), 1, Seite 59-62 |
| Übergeordnetes Werk: |
volume:324 ; year:1993 ; number:1 ; pages:59-62 |
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NLEJ173359906 |
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| 245 | 1 | 0 | |a Purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells |
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| 520 | |a The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. | ||
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| 700 | 1 | |a Hekman, M. |4 oth | |
| 700 | 1 | |a Buchen, C. |4 oth | |
| 700 | 1 | |a Elce, J.S. |4 oth | |
| 700 | 1 | |a Lohse, M.J. |4 oth | |
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(DE-627)NLEJ173359906 (DE-599)GBVNLZ173359906 DE-627 ger DE-627 rakwb eng Purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Sohlemann, P. oth Hekman, M. oth Buchen, C. oth Elce, J.S. oth Lohse, M.J. oth in FEBS Letters Amsterdam : Elsevier 324(1993), 1, Seite 59-62 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:324 year:1993 number:1 pages:59-62 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81532-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 324 1993 1 59-62 |
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(DE-627)NLEJ173359906 (DE-599)GBVNLZ173359906 DE-627 ger DE-627 rakwb eng Purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Sohlemann, P. oth Hekman, M. oth Buchen, C. oth Elce, J.S. oth Lohse, M.J. oth in FEBS Letters Amsterdam : Elsevier 324(1993), 1, Seite 59-62 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:324 year:1993 number:1 pages:59-62 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81532-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 324 1993 1 59-62 |
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(DE-627)NLEJ173359906 (DE-599)GBVNLZ173359906 DE-627 ger DE-627 rakwb eng Purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Sohlemann, P. oth Hekman, M. oth Buchen, C. oth Elce, J.S. oth Lohse, M.J. oth in FEBS Letters Amsterdam : Elsevier 324(1993), 1, Seite 59-62 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:324 year:1993 number:1 pages:59-62 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81532-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 324 1993 1 59-62 |
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(DE-627)NLEJ173359906 (DE-599)GBVNLZ173359906 DE-627 ger DE-627 rakwb eng Purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Sohlemann, P. oth Hekman, M. oth Buchen, C. oth Elce, J.S. oth Lohse, M.J. oth in FEBS Letters Amsterdam : Elsevier 324(1993), 1, Seite 59-62 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:324 year:1993 number:1 pages:59-62 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81532-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 324 1993 1 59-62 |
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(DE-627)NLEJ173359906 (DE-599)GBVNLZ173359906 DE-627 ger DE-627 rakwb eng Purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Sohlemann, P. oth Hekman, M. oth Buchen, C. oth Elce, J.S. oth Lohse, M.J. oth in FEBS Letters Amsterdam : Elsevier 324(1993), 1, Seite 59-62 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:324 year:1993 number:1 pages:59-62 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81532-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 324 1993 1 59-62 |
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purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells |
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Purification and functional characterization of β-adrenergic receptor kinase expressed in insect cells |
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The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. |
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The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. |
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The β-adrenergic receptor kinase mediates agonist-dependent phosphorylation of β-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human βARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The K"m-values of the enzyme were 3.8 μM for rhodopsin and 22 μM for ATP; the V"m"a"x-value was 9.9 mol phosphate/mol βARK/min. These data indicate that the two recombinant kinases were at least as active as preparations previously obtained from bovine brain. There were no differences in the functional activity of human and bovine βARK. |
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