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A 32‐kDa protein associated with phospholipase A 2 ‐inhibitory activity from human placenta
Author(s) -
Hayashi Hideki,
Owada M.Koji,
Sonobe Seiji,
Kakunaga Takeo,
Kawakatsu Hisaaki,
Yano Junichi
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80302-2
Subject(s) - chemistry , human placenta , inhibitory postsynaptic potential , biochemistry , placenta , peptide , biology , endocrinology , fetus , pregnancy , genetics
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.