title: Identification of a new phosphorylation site in cardiac muscle phosphofructokinase.
abstract: The novel phosphorylation site (Ser376) that we discovered during in vitro studies of the troponin C- or calmodulin-induced phosphorylation of rabbit muscle phosphofructokinase [Zhao, Z., Malencik, D.A., and Anderson, S. R. (1991) Biochemistry 30, 2204] also undergoes phosphorylation in the epinephrine-stimulated rabbit heart. Reversed-phase HPLC and/or iron chelate affinity chromatography performed on CNBr digests of phosphofructokinase that had been isolated from epinephrine-treated hearts yields a largely phosphorylated peptide corresponding to amino acid residues 371-378 of the enzyme. Mass spectrometry, gas phase sequencing, and amino acid analyses establish the structure and phosphorylation state of the peptide.
authors.affiliation: Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331, USA.
authors.forename: J J
authors.initials: JJ
authors.lastname: Harrahy
authors.forename: D A
authors.initials: DA
authors.lastname: Malencik
authors.forename: Z
authors.initials: Z
authors.lastname: Zhao
authors.forename: F L
authors.initials: FL
authors.lastname: Hisaw
authors.forename: S R
authors.initials: SR
authors.lastname: Anderson
mesh_terms: D000818:Animals; D002851:Chromatography, High Pressure Liquid; D009206:Myocardium / Q000201:enzymology*; D010449:Peptide Mapping; D010732:Phosphofructokinase-1 / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D011817:Rabbits; D012694:Serine / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D012694:Serine; D010732:Phosphofructokinase-1