Mammalian pancreatic phospholipase A2 (PLA2-I) has its specific receptor through which PLA2-I induces a variety of biological responses. In this study, a fundamental relationship between the enzymatic and the receptor-binding activities of PLA2-I was investigated. The specific binding of PLA2-I to the receptor was found to be independent of Ca2+ which is requisite for the PLA2 activity. On the basis of this observation, we designed and produced mutant PLA2-Is without Ca2+-binding abilities in order to demonstrate that the structural requirement for the enzymatic activity of PLA2-I is not identical with that for its receptor-binding reaction. These mutant PLA2-Is lost almost all enzymatic activity through a disturbance at the Ca2+-binding site, as expected, but still retained a substantial affinity to the receptor, allowing us to conclude that the receptor-binding reaction of PLA2-I is separable from its catalytic action.
