Stimulation of enzyme activities by fragments of calmodulin

In this paper the ability of Ca super(2+) binding sites to activate phoshorylase kinase and cyclic nucleotide phosphodiesterase has been compared, as well as their ability to substitute for troponin-C in neutralizing the inhibition of actomyosin-ATPase by troponin-I. These studies demonstrate that m...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	FEBS letters 1981-07, Vol.130 (1), p.141-145
Hauptverfasser:	Kuznicki, J., Grabarek, Z., Brzeska, H., Drabikowski, W., Cohen, Philip
Format:	Artikel
Sprache:	eng
Schlagworte:	3',5'-Cyclic-AMP Phosphodiesterases - metabolism 3':5'-Cyclic-nucleotide phosphodiesterase Actomyosin - metabolism adenosine triphosphatase Adenosine Triphosphatases - metabolism Animals Calcium-Binding Proteins - pharmacology calmodulin Calmodulin - pharmacology Cattle Dose-Response Relationship, Drug Enzyme Activation - drug effects enzymes Peptide Fragments - pharmacology peptides phosphorylase kinase Phosphorylase Kinase - metabolism Rabbits Trifluoperazine - pharmacology Troponin - pharmacology Troponin I
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	In this paper the ability of Ca super(2+) binding sites to activate phoshorylase kinase and cyclic nucleotide phosphodiesterase has been compared, as well as their ability to substitute for troponin-C in neutralizing the inhibition of actomyosin-ATPase by troponin-I. These studies demonstrate that more than one region of the calmodulin molecule is capable on interacting with its target proteins, and that different calmodulin-dependent proteins do not interact with calmodulin in an identical manner.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(81)80683-7