| Literature DB >> 19673083 |
Ryoichi Shirai1, Michihisa Toriba, Kyozo Hayashi, Kiyoshi Ikeda, Seiji Inoue.
Abstract
Two distinct phospholipase A2 (PLA2) inhibitory proteins (PLIs) were purified from the serum of the Japanese rat snake, Elaphe climacophora. The 150-kDa inhibitor, a trimer of a 50-kDa subunit, specifically inhibited the basic PLA2 purified from the venom of Gloydius brevicaudus, whereas the 120-kDa one composed of two distinct 25-kDa subunits. A and B, inhibited both the acidic and basic PLA2s of G. brevicaudus. On the basis of their amino acid sequences, these inhibitors were assigned as PLI beta and PLI gamma, respectively. A PLI alpha homolog (PLI alpha-like protein; PLI alpha-LP) having an apparent molecular weight of 50-kDa and composed of 15-kDa subunits was also purified from the E. climacophora serum. This homolog was immunoreactive with antibody raised against the G. brevicaudus PLI alpha, but lacked in the inhibitory activity toward the acidic and basic PLA2s. The cDNAs encoding PLI alpha-LP, PLI beta, PLI gamma-A, and PLI gamma-B were cloned from liver RNA, and their nucleotide sequences were compared with those of other venomous and non-venomous snakes.Entities:
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Year: 2009 PMID： 19673083 DOI： 10.1016/j.toxicon.2009.02.001
Source DB: PubMed Journal: Toxicon ISSN： 0041-0101 Impact factor: 3.033