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Amino acid sequence at the phosphorylated site of rat liver pyruvate kinase

Biochemical and Biophysical Research CommunicationsPublished 1 December 1975
Bror Edlund, Jill Andersson, Vincent P. K. Titanji, Ulla Dahlqvist, Pia Ekman, Örjan Zetterqvist
Citations50
SJR quartileQ2
SJR score0.75
SNIP0.56

TL;DR

One dominating peptic phosphopeptide was obtained from rat liver pyruvate kinase (type L) phosphorylated by cyclic 3′,5′-AMP-stimulated protein kinase from the same tissue.

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.

Keywords

Biochemistry, Genetics and Molecular Biology