Premium
The interaction of phospholipase A2 with liposomes: An immunological approach to its study
Author(s) -
Morales Rogelio,
Zavala Eunice,
Fernández Marta S.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202182
Subject(s) - liposome , phosphatidylcholine , vesicle , antiserum , phospholipase a2 , polyclonal antibodies , chemistry , phospholipase a , membrane , chromatography , enzyme , biophysics , biochemistry , antibody , phospholipid , biology , immunology
Porcine pancreatic phospholipase A2 (PLA2) has been incubated for 2 hours at 34°C with rabbit anti‐pig pancreatic PLA2 polyclonal antiserum in the absence or presence of phosphatidylcholine liposomes in different physical states. Subsequent assay of hydrolysis ‐triggered through addition of 5 mM Ca2+‐ at 34°C, shows that preincubation with antiserum in the presence of 1,2‐dimyristoyl‐3‐sn‐phosphatidylcholine liquid‐crystalline vesicles, renders the PLA2 activity undetectable, similarly to what is found if preincubation is carried out in the absence of liposomes. In contrast, 1,2‐dipalmitoyl‐3‐sn‐phosphatidylcholine liposomes, which at 34°C are in the gel‐phase, protect the enzyme from the antiserum effect. The results are consistent with a stronger binding of PLA2 to gel phase, as compared to liquid crystalline vesicles and suggest that through the physical interaction with liposomes in the gel state, the enzyme is shielded from reaction with the antibodies. Taking into account the characteristic hydrolysis profiles of vesicles in different physical states, it can be concluded that the above interpretation agrees with the proposal that PLA2‐membrane association promotes the interfacial activation of the enzyme.