-transparent.png){kind=logo}
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.
Related Publications
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
July 1987,
FEBS letters,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
October 1995,
The Biochemical journal,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
April 1997,
The Journal of endocrinology,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
October 1989,
Cell structure and function,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
January 1987,
Advances in prostaglandin, thromboxane, and leukotriene research,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
April 1998,
The Journal of endocrinology,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
July 1987,
Biochemical and biophysical research communications,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
April 1992,
Journal of chromatography,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
October 1997,
The Biochemical journal,
H Hayashi, and
M K Owada, and
S Sonobe, and
T Kakunaga, and
H Kawakatsu, and
J Yano
June 1989,
Nihon Naibunpi Gakkai zasshi,
