A 32-kDa protein associated with phospholipase A2-inhibitory activity from human placenta |
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Authors: | H Hayashi M K Owada S Sonobe T Kakunaga H Kawakatsu J Yano |
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Affiliation: | Department of Oncogene Research, Osaka University, Japan. |
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Abstract: | 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. |
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