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Amino acid sequence at the phosphorylated site of rat liver pyruvate kinase
Authors:Bror Edlund  Jill Andersson  Vincent Titanji  Ulla Dahlqvist  Pia Ekman  Örjan Zetterqvist  Lorentz Engström
Affiliation:Institute of Medical and Physiological Chemistry, Biomedical Center, University of Uppsala, S-751 23 Uppsala, Sweden
Abstract:One dominating peptic phosphopeptide, Asx-Thr-Lys-Gly-Pro-Glx-Ile-Glx-Thr-Gly-Val-Leu-Arg-Arg-Ala-(32P)SerP-Val-Ala-Glx-Leu, was obtained from rat liver pyruvate kinase (type L) phosphorylated by cyclic 3′,5′-AMP-stimulated protein kinase from the same tissue. The sequence around the phosphorylated serine residue is similar to that of a corresponding but smaller peptic phosphopeptide previously isolated from pig liver (type L) pyruvate kinase, Leu-Arg-Arg-Ala-(32P)SerP-Leu.
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