A 32-kDa protein associated with phospholipase A2-inhibitory activity from human placenta.
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.
Hayashi
H
H
Department of Oncogene Research, Osaka University, Japan.
Owada
M K
MK
Sonobe
S
S
Kakunaga
T
T
Kawakatsu
H
H
Yano
J
J
D004791:Enzyme Inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007526:Isoelectric Point; D008970:Molecular Weight; D010449:Peptide Mapping; D010740:Phospholipases / Q000037:antagonists & inhibitors*; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2; D010920:Placenta / Q000201:enzymology*; D014018:Tissue Distribution
D004791:Enzyme Inhibitors; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2