%0 Journal Article %1 Sohlemann1993 %A Sohlemann, P. %A Hekman, M. %A Buchen, C. %A Elce, J. S. %A Lohse, M. J. %D 1993 %J FEBS Lett %K & *Cyclic AMP-Dependent Adenosine Animals Cell Chromatography, Cloning, Exchange Gel Humans Ion Kinases Kinases/genetics/*isolation Kinetics Line Molecular Moths Outer Phosphorylation Protein Proteins/isolation Receptor Recombinant Rhodopsin/metabolism Rod Segment/metabolism Transfection Triphosphate/metabolism beta-Adrenergic purification/*metabolism purification/metabolism %N 1 %P 59-62 %T Purification and functional characterization of beta-adrenergic receptor kinase expressed in insect cells %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8504860 %V 324 %X The beta-adrenergic receptor kinase mediates agonist-dependent phosphorylation of beta-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human beta ARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The Km-values of the enzyme were 3.8 microM for rhodopsin and 22 microM for ATP; the Vmax-value was 9.9 mol phosphate/mol beta ARK/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 beta ARK.

@article{Sohlemann1993, abstract = {The beta-adrenergic receptor kinase mediates agonist-dependent phosphorylation of beta-adrenergic receptors, which is thought to represent the first step of homologous desensitization. We have expressed bovine and human beta ARK1 in Sf9 cells and purified them to apparent homogeneity in milligram quantities. The Km-values of the enzyme were 3.8 microM for rhodopsin and 22 microM for ATP; the Vmax-value was 9.9 mol phosphate/mol beta ARK/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 beta ARK.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {Sohlemann, P. and Hekman, M. and Buchen, C. and Elce, J. S. and Lohse, M. J.}, biburl = {https://www.bibsonomy.org/bibtex/2054134af7cf23973654809c6a198e3d1/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {100efefa822dcabef5a65d3f19b2dd43}, intrahash = {054134af7cf23973654809c6a198e3d1}, issn = {0014-5793 (Print) 0014-5793 (Linking)}, journal = {FEBS Lett}, keywords = {& *Cyclic AMP-Dependent Adenosine Animals Cell Chromatography, Cloning, Exchange Gel Humans Ion Kinases Kinases/genetics/*isolation Kinetics Line Molecular Moths Outer Phosphorylation Protein Proteins/isolation Receptor Recombinant Rhodopsin/metabolism Rod Segment/metabolism Transfection Triphosphate/metabolism beta-Adrenergic purification/*metabolism purification/metabolism}, month = {Jun 7}, note = {Sohlemann, P Hekman, M Buchen, C Elce, J S Lohse, M J Comparative Study Research Support, Non-U.S. Gov't Netherlands FEBS letters FEBS Lett. 1993 Jun 7;324(1):59-62.}, number = 1, pages = {59-62}, shorttitle = {Purification and functional characterization of beta-adrenergic receptor kinase expressed in insect cells}, timestamp = {2010-12-14T18:22:03.000+0100}, title = {Purification and functional characterization of beta-adrenergic receptor kinase expressed in insect cells}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8504860}, volume = 324, year = 1993 }