Modification of kinetic parameters of glycogen phosphorylase from mantle tissue of Mytilus galloprovincialis by a phosphorylation mechanism

Initial rate and affinity studies on mantle Mytilus phosphorylase a were carried out in order to find possible differences in its kinetic properties with respect to phosphorylase b. Phosphorylase a was not stimulated for any AMP concentrations. Michaelis constants ( K m) are 0.05 mg/ml glycogen, 1.1...

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Veröffentlicht in:	The international journal of biochemistry & cell biology 1995-09, Vol.27 (9), p.917-922
Hauptverfasser:	Serrano, Fuencisla San Juan, González, Margarita Fernández, López, JoséLuis Sánchez, Martín, L.Oscar Garcia
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Monophosphate - pharmacology Animals Bivalvia - enzymology Glycogen - metabolism Kinetic parameters Kinetics Mytilus Phosphates - metabolism Phosphorylase Phosphorylase a - metabolism Phosphorylase b - metabolism Phosphorylases - metabolism Phosphorylation Substrate Specificity
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