Open AccessInteraction of Phospolipase A 2 form Naja melanoleuca Sanke Venom with Meoomeric Substrate Analogs
Author(s) -
EIJK Jan H.,
VERHEIJ Hubertus M.,
DIJKMAN Ruud,
HAAS Gerared H.
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07345.x
Subject(s) - venom , substrate (aquarium) , micelle , enzyme , chemistry , snake venom , phospholipase , critical micelle concentration , stereochemistry , biophysics , biochemistry , organic chemistry , biology , ecology , aqueous solution
Unlike porcine pancreatic phospholipase A 2 , the enzyme from Naja melanoleuca does not display bisphaisc kinetic behaviour at substrate concentrations around the critical concentration. This snake venom enzyme was further investigateds around the critical micelle cnentration. This snake vemom enyme was futher investigated by dirct biding studes using n ‐tridecylphosphochline. Binding of this substrate analog to the enzyme was monitored by using equilibrium gel filtration, equilibrium dialyssis and ultraviolet difference spectroswcopy. It is concluded that, in the presence of submicellar conenraitons of n ‐tridecylphosphocholin, a lipid‐pritien complex is formed cosisting of about 4 protein and 36 lipid molecules. Ca 2+ ions are required for the formation of this complex. A model is proposed which describes the formation of this type of complex. Thsse lipidfomramtion of this complez. A model is proposed which describes th formation of this type of compelex. These lipid protein aggregates are held responsible for the non‐hyperbolic kinetic behaviour of the skanke venom enzyme towards monomeric substrates.