The acidic peptide-specific type II protein kinases from the nucleus and the cytosol of porcine liver are distinct |
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| Authors: | H Baydoun F Feth J Hoppe H Erdmann K G Wagner |
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| Affiliation: | 1. Institute of Epidemiology and Social Medicine, University of Münster, Münster, Germany;2. Discipline of Psychiatry, University of Adelaide, Adelaide, Australia;3. Department of Neurology, University of Munich, Munich, Germany;1. DeBartolo Family Personalised Medicine Institute, H Lee Moffitt Cancer Center and Research Institute, Tampa, FL, USA;2. Department of Cancer Epidemiology, H Lee Moffitt Cancer Center and Research Institute, Tampa, FL, USA;3. Department of Malignant Hematology, H Lee Moffitt Cancer Center and Research Institute, Tampa, FL, USA;4. Department of Biostatistics and Bioinformatics, H Lee Moffitt Cancer Center and Research Institute, Tampa, FL, USA;5. Molecular Genomics Core, H Lee Moffitt Cancer Center and Research Institute, Tampa, FL, USA;6. Center for Pharmacogenomics and Individualised Therapy, Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, NC, USA;1. Department of Biochemistry, Yuvaraja''s College, University of Mysore, Mysuru, 570005, Karnataka, India;2. Department of Basic Sciences, Deanship of Preparatory Year and Supporting Studies, Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam, 34212, Saudi Arabia;3. Department of Biotechnology, Yuvaraja''s College, University of Mysore, Mysuru, 570005, Karnataka, India;1. Univ Lyon, University Claude Bernard Lyon 1, L-VIS, F-69622, Lyon, France;2. University of Valencia, Department of Sociology and Social Anthropology, Faculty of Social Sciences, Avd. de los Naranjos 4b, Office 4D20, 46021, Valencia, Spain;1. School of Physics & Astronomy, University of Edinburgh, James Clerk Maxwell Building, Peter Guthrie Tait Road, Edinburgh EH9 3FD, UK;2. ISIS Neutron & Muon Source, Rutherford Appleton Laboratory, Harwell, Oxford OX11 0XX, UK |
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| Abstract: | The second messenger-independent acidic peptide-specific protein kinase II (casein kinase II) from the cytosol of porcine liver has been purified to apparent homogeneity by using DEAE-cellulose, hydroxyl apatite, and phosphocellulose chromatography. The native enzyme has an apparent Mr of 150,000. After sodium dodecyl sulfate-gel electrophoresis a band of Mr = 39,000 and a slightly diffuse band of Mr = 27,000 were found indicating an alpha 2 beta 2 structure of this protein kinase. A thorough comparison with the corresponding enzyme from the nucleus was performed. The two enzymes differ in the subunit composition, as the nuclear enzyme is composed of subunits with a Mr of 95,000; they further differ in the heparin sensitivity and binding to blue dextran-Sepharose. Distinct differences in their nucleotide binding sites were found upon mapping with ATP analogs, although both enzymes utilize ATP as well as GTP. On the other hand, both enzymes phosphorylate identical sites in the casein variants beta A2 and alpha S1B at comparable rates. These results demonstrate for the first time the existence of distinct nucleus and cytoplasm specific type II "casein kinases". |
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