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In vitro phosphorylation of serum albumin by two protein kinases:  a potential pitfall in protein phosphorylation reactions
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry.
1986 (English)In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 154, no 2, 395-399 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
1986. Vol. 154, no 2, 395-399 p.
Keyword [en]
protein kinases, phosphate compounds, autoradiography, albumin
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-172747DOI: 10.1016/0003-2697(86)90004-7OAI: oai:DiVA.org:uu-172747DiVA: diva2:515516
Available from: 2012-04-13 Created: 2012-04-13 Last updated: 2017-12-07Bibliographically approved

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Ekman, Pia

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