Phosphofructokinase is a calmodulin binding protein.
Standard
Phosphofructokinase is a calmodulin binding protein. / Mayr, Georg W.; Heilmeyer, L M.
in: FEBS LETT, Jahrgang 159, Nr. 1-2, 1-2, 1983, S. 51-57.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
Harvard
APA
Vancouver
Bibtex
}
RIS
TY - JOUR
T1 - Phosphofructokinase is a calmodulin binding protein.
AU - Mayr, Georg W.
AU - Heilmeyer, L M
PY - 1983
Y1 - 1983
N2 - A trial to purify myosin light chain kinase from crude myosin led to the isolation of a Mr 85 000 calmodulin binding protein different from this enzyme. Because it showed inherent phosphofructokinase activity we investigated its relation to this enzyme. We demonstrated identity to phosphofructokinase by a close to identical amino acid composition, by antigenic identity and a set of completely identical peptide maps. The calmodulin binding property was also shown for a fraction of the enzyme prepared by standard methods. First experiments show that Ca2+--calmodulin is a potent regulator of phosphofructokinase polymerization.
AB - A trial to purify myosin light chain kinase from crude myosin led to the isolation of a Mr 85 000 calmodulin binding protein different from this enzyme. Because it showed inherent phosphofructokinase activity we investigated its relation to this enzyme. We demonstrated identity to phosphofructokinase by a close to identical amino acid composition, by antigenic identity and a set of completely identical peptide maps. The calmodulin binding property was also shown for a fraction of the enzyme prepared by standard methods. First experiments show that Ca2+--calmodulin is a potent regulator of phosphofructokinase polymerization.
M3 - SCORING: Zeitschriftenaufsatz
VL - 159
SP - 51
EP - 57
JO - FEBS LETT
JF - FEBS LETT
SN - 0014-5793
IS - 1-2
M1 - 1-2
ER -
