HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Institute of Low Temperature Science >
Peer-reviewed Journal Articles, etc >

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

Files in This Item:
pnas101.pdf573.55 kBPDFView/Open
Please use this identifier to cite or link to this item:

Title: Blarina toxin, a mammalian lethal venom from the short-tailed shrew Blarina brevicauda : Isolation and characterization
Authors: Kita, Masaki Browse this author
Nakamura, Yasuo Browse this author
Okumura, Yuushi Browse this author
Ohdachi, Satoshi D. Browse this author →KAKEN DB
Oba, Yuichi Browse this author
Yoshikuni, Michiyasu Browse this author
Kido, Hiroshi Browse this author
Uemura, Daisuke Browse this author
Issue Date: 18-May-2004
Publisher: The National Academy of Sciences
Journal Title: Proceedings of the National Academy of Sciences
Volume: 101
Issue: 20
Start Page: 7542
End Page: 7547
Publisher DOI: 10.1073/pnas.0402517101
PMID: 15136743
Abstract: 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.
Type: article (author version)
Appears in Collections:低温科学研究所 (Institute of Low Temperature Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 大舘 智志

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 - Hokkaido University