In vitro phosphorylation of serum albumin by two protein kinases: a potential pitfall in protein phosphorylation reactions |
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| Authors: | S C Martin P Ekman |
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| Affiliation: | 1. Cancer Research Division, Cancer Council NSW, Sydney, Australia;2. Sydney School of Public Health, University of Sydney, Sydney, Australia;3. School of Medicine and Public Health, University of Newcastle, Newcastle, Australia;1. Department of Cytophysiology, Chair of Histology and Embryology, School of Medicine in Katowice, Medical University of Silesia, Medyków 18, 40-758 Katowice, Poland;2. Students Scientific Society, School of Medicine in Katowice, Medical University of Silesia, Medyków 18, 40-758 Katowice, Poland;1. Department of Translational Research and New Technologies in Medicine and Surgery, Unit of Medical Oncology 2, Azienda Ospedaliera Universitaria Pisana, Pisa, Italy;2. Medical Oncology Department, Fondazione IRCCS Istituto Nazionale dei Tumori, Milan, Italy;3. Unit of Medical Oncology 1, Department of Clinical and Experimental Oncology, Veneto Institute of Oncology, IOV-IRCCS, Department of Surgery, Oncology and Gastroenterology, University of Padua, Padua, Italy;4. Department of Medical Oncology, Campus Bio-Medico, University of Rome, Rome, Italy;5. Fondazione Policlinico Universitario A. Gemelli, IRCCS-UOC Oncologia Medica, Rome, Italy;6. Medical Oncology Department, University Hospital, University of Cagliari, Cagliari, Italy;7. Unit of Medical Oncology 1, Department of Clinical and Experimental Oncology, Veneto Institute of Oncology, IOV-IRCCS, Padua, Italy;1. Department of Pathology and Molecular Medicine, McMaster Immunology Research Centre, Institute for Infectious Disease Research, McMaster University, Hamilton, Ontario, Canada |
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| Abstract: | Bovine albumin was phosphorylated by both cAMP-dependent protein kinase and casein kinase I to a significant extent. Other albumins were also tested and it was found that the extent of phosphorylation varied with the species of origin of the albumin, but was between 1 and 3 mol phosphate per mole albumin for the cAMP-dependent protein kinase-catalyzed reactions. The phosphorylation occurred at and above pH 7.5 and required the presence of thiol reagents. Phosphoamino acid analyses of bovine albumin showed that it was phosphorylated on at least two serine residues. The phosphorylation could not be demonstrated in vivo. |
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