A 32‐kDa protein associated with phospholipase A2‐inhibitory activity from human placenta

FEBS Letters

Kakunaga, Takeo³  Kawakatsu, Hisaaki²  Sonobe, Seiji³  Yano, Junichi²  Hayashi, Hideki³  Owada, M.Koji¹ 

[1] Tumor Virology, Research Institute for Microbial Diseases, Osaka University, 3-1, Yamada-oka, Suita, Osaka 565, Japan;Research Laboratories, Nippon Shinyaku Co., Ltd, Nishiohji Hachijo, Minamiku, Kyoto 601, Japan;Departments of Oncogene Research and Research Institute for Microbial Diseases, Osaka University, 3-1, Yamada-oka, Suita, Osaka 565, Japan

关键词: 32-kDa protein;    Phospholipase A2;    Enzyme inhibitor;    Ca2+-dependent phospholipid binding;    Calpactin;    Lipocortin;    (Human placenta);    PLA2;    phospholipase A2;    CNBr;    cyanogen bromide;    PS;    phosphatidylserine;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    EGF;    epidermal growth factor;   

DOI  :  10.1016/0014-5793(87)80302-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown