Blarina toxin, a mammalian lethal venom from the short-tailed shrew Blarina brevicauda : Isolation and characterization

Kita, Masaki; Nakamura, Yasuo; Okumura, Yuushi; Ohdachi, Satoshi D.; Oba, Yuichi; Yoshikuni, Michiyasu; Kido, Hiroshi; Uemura, Daisuke

Blarina toxin, a mammalian lethal venom from the short-tailed shrew Blarina brevicauda : Isolation and characterization

Kita, Masaki; Nakamura, Yasuo; Okumura, Yuushi et al.

Proceedings of the National Academy of Sciences, 2004, 101(20), 7542-7547

Permalink : https://hdl.handle.net/2115/44382

このアイテムのアクセス数:1,344件（2026-08-24 20:57 集計）

閲覧可能ファイル

ファイル	フォーマット	サイズ	閲覧回数	説明
nas101	pdf	573 KB	1,052

論文情報

ファイル出力 EndNote Basic出力 Mendeley出力

アクセス権	open access
URI	https://hdl.handle.net/2115/44382
タイトル	Blarina toxin, a mammalian lethal venom from the short-tailed shrew Blarina brevicauda : Isolation and characterization
著者	Kita, Masaki ; Nakamura, Yasuo ; Okumura, Yuushi ; Ohdachi, Satoshi D. ; Oba, Yuichi ; Yoshikuni, Michiyasu ; Kido, Hiroshi ; Uemura, Daisuke
著者名 Kita, Masaki
著者名 Nakamura, Yasuo
著者名 Okumura, Yuushi
e-Rad_Researcher 60292041 著者名 Ohdachi, Satoshi D.
著者名 Oba, Yuichi
著者名 Yoshikuni, Michiyasu
著者名 Kido, Hiroshi
著者名 Uemura, Daisuke
言語	英語
発行日	2004-05-18
出版者	The National Academy of Sciences
収録物名	Proceedings of the National Academy of Sciences
巻(号)	101(20)
ページ	7542-7547
抄録	Venomous mammals are rare, and their venoms have not been characterized. We have purified and characterized the blarina toxin (BLTX), a lethal mammalian venom with a tissue kallikrein-like activity from the submaxillary and sublingual glands of the short-tailed shrew Blarina brevicauda. Mice administered BLTX i.p. developed irregular respiration, paralysis, and convulsions before dying. Based on the amino acid sequence of purified protein, we cloned the BLTX cDNA. It consists of a prosequence and an active form of 253 aa with a typical catalytic triad of serine proteases, with a high identity with tissue kallikreins. BLTX is an N-linked microheterogeneous glycoprotein with a unique insertion of 10 residues, L106TFFYKTFLG115. BLTX converted kininogens to kinins, which may be one of the toxic pathogens, and had dilatory effects on the blood vessel walls. The acute toxicity and proteolytic activity of BLTX were strongly inhibited by aprotinin, a kallikrein inhibitor, suggesting that its toxicity is due to a kallikrein-like activity of the venom.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
関連情報	PMID 15136743
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1073/pnas.0402517101