Hayashi H, Owada M K, Sonobe S, Kakunaga T, Kawakatsu H, Yano J
Department of Oncogene Research, Osaka University, Japan.
FEBS Lett. 1987 Nov 2;223(2):267-72. doi: 10.1016/0014-5793(87)80302-2.
Two monomeric 32-kDa proteins, termed 32K-I (pI 5.8) and 32K-II (pI 5.1), were isolated from human placenta, which was solubilized by a Ca2+-chelator. Only 32K-I was associated with PLA2-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 PLA2-inhibitory activity. 32K-I bound to PS in a Ca2+-dependent manner. 32K-I was detected in many tissues except brain, cardiac and skeletal muscle.
