Abstract
Two monomeric 32-kDa proteins, termed 32K-I (p I 5.8) and 32K-II (p I 5.1), were isolated from human placenta, which was solubilized by a Ca 2+-chelator. Only 32K-I was associated with PLA 2-inhibitory activity. CNBr peptide mapping indicated that 32K-I was distinct from 32K-II and two 36-kDa proteins, called calpactin I and II or lipocortin II and I, which have been shown to possess PLA 2-inhibitory activity. 32K-I bound to PS in a Ca 2+-dependent manner. 32K-I was detected in many tissues except brain, cardiac and skeletal muscle.
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