Competitive inhibition of lipolytic enzymes. XI. Estimation of the interfacial dissociation constants of porcine pancreatic phospholipase A2 for substrate and inhibitor in the absence of detergents.
Based on the strong inhibitory properties of (R)-2-decanoylamino-octanol-1-phosphocholine and its phosphoglycol analogue for porcine pancreatic phospholipase A2, the corresponding 2-decanoyloxy derivatives have been synthesised in both enantiomeric forms and their substrate properties for the enzyme were analysed. The high aqueous solubility in the absence of detergents, combined with low critical micelle concentrations of both the amide- and ester phospholipids allowed the estimation of the interfacial dissociation constants of the enzyme-substrate and enzyme-inhibitor complexes by kinetic and direct binding techniques.
De Haas
G H
GH
Department of Enzymology and Protein Engineering, C.B.L.E., Utrecht, The Netherlands.
Dijkman
R
R
Boots
J W
JW
Verheij
H M
HM
D000818:Animals; D001667:Binding, Competitive; D003902:Detergents; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology*; D010741:Phospholipases A / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D054467:Phospholipases A2; D010743:Phospholipids / Q000138:chemical synthesis / Q000378:metabolism; D013237:Stereoisomerism; D013379:Substrate Specificity; D013552:Swine
D003902:Detergents; D010743:Phospholipids; D010741:Phospholipases A; D054467:Phospholipases A2