Modulation of phospholipases A2 and C activities against dilauroylphosphorylcholine in mixed monolayers with semisynthetic derivatives of ganglioside and sphingosine

Summary Most of the semisynthetic ganglioside and sphingosine derivatives studied here decreased the rate as well as the extent of hydrolysis of monomolecular layers of dilauroylphosphorylcholine (dIPC) by both phospholipase A2 (PLA2) and C (PLC). For PLA2, the rate of enzymatic activity was inverse...

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Veröffentlicht in:	Molecular membrane biology 1994, Vol.11 (2), p.119-126
Hauptverfasser:	Perillo, Marí A., Guidotti, Alessandro, Costa, Erminio, Yu, Robert K., Maggio, Bruno
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences Carbohydrate Sequence Cell Membrane - metabolism Electrochemistry Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology gangliosides Gangliosides - chemistry Gangliosides - metabolism Hydrolases In Vitro Techniques Kinetics Models, Biological Molecular Sequence Data monolayers Phosphatidylcholines - metabolism Phospholipase A phospholipase C Phospholipases A - metabolism Phospholipases A2 Signal Transduction Sphingosine - chemistry Sphingosine - metabolism sphingosine derivatives Type C Phospholipases - metabolism
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Zusammenfassung:	Summary Most of the semisynthetic ganglioside and sphingosine derivatives studied here decreased the rate as well as the extent of hydrolysis of monomolecular layers of dilauroylphosphorylcholine (dIPC) by both phospholipase A2 (PLA2) and C (PLC). For PLA2, the rate of enzymatic activity was inversely correlated (p
ISSN:	0968-7688 1464-5203
DOI:	10.3109/09687689409162229