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Amino acid sequence at the phosphorylated site of rat liver pyruvate kinase
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (Engström Lorentz)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (Engsröm Lorentz)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (Engström Lorentz)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (Engström Lorentz)
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1975 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 67, no 4, 1516-1521 p.Article in journal (Refereed) Published
Abstract [en]

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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1975. Vol. 67, no 4, 1516-1521 p.
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Other Basic Medicine
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URN: urn:nbn:se:uu:diva-169172DOI: 10.1016/0006-291X(75)90198-9PubMedID: 1106423OAI: oai:DiVA.org:uu-169172DiVA: diva2:505255
Available from: 2012-02-23 Created: 2012-02-23 Last updated: 2017-12-07Bibliographically approved

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Dahlqvist, UllaEkman, Pia

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