Correlation between Multiple Phosphorylation of Gizzard Myosin Light Chains and Actin-Activated Myosin ATPase Activity

With large amounts of gizzard Mr 135,000 calmodulin-binding protein (myosin light chain kinase), the phosphate incorporation into myosin light chains was determined to be 2 mol/mol of myosin light chain. The actin-activated ATPase activity was dramatically enhanced when myosin light chains were phos...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Journal of biochemistry (Tokyo) 1985-01, Vol.97 (6), p.1823-1826
Hauptverfasser:	TANAKA, Toshihiko, YAMAZAKI, Keiji, SOBUE, Kenji
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - physiology Adenosine Triphosphatases - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Chickens Contractile proteins Enzyme Activation Fundamental and applied biological sciences. Psychology Gizzard, Avian - metabolism Holoproteins Myosin-Light-Chain Kinase Phosphorylation Protein Kinases - metabolism Proteins
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	With large amounts of gizzard Mr 135,000 calmodulin-binding protein (myosin light chain kinase), the phosphate incorporation into myosin light chains was determined to be 2 mol/mol of myosin light chain. The actin-activated ATPase activity was dramatically enhanced when myosin light chains were phosphorylated by more than 1 mol of phosphate incorporated/mol of myosin light chain.
ISSN:	0021-924X 1756-2651
DOI:	10.1093/oxfordjournals.jbchem.a135244