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Purification and characterisation of blarinasin, a new tissue kallikrein-like protease from the short-tailed shrew Blarina brevicauda: comparative studies with blarina toxin

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Title: Purification and characterisation of blarinasin, a new tissue kallikrein-like protease from the short-tailed shrew Blarina brevicauda: comparative studies with blarina toxin
Authors: Kita, Masaki Browse this author
Okumura, Yuushi Browse this author
Ohdachi, Satoshi D.3 Browse this author →KAKEN DB
Oba, Yuichi Browse this author
Yoshikuni, Michiyasu Browse this author
Nakamura, Yasuo Browse this author
Kido, Hiroshi Browse this author
Uemura, Daisuke Browse this author
Authors(alt): 大舘, 智志3
Keywords: Amino acid sequence analysis
Blarinasin
Blarina toxin
Salivary glands
Short-tailed shrew
Tissue kallikrein
Issue Date: Feb-2005
Publisher: Walter de Gruyter
Journal Title: Biological Chemistry
Volume: 386
Issue: 2
Start Page: 177
End Page: 182
Publisher DOI: 10.1515/BC.2005.022
Abstract: A new tissue kallikrein-like protease, blarinasin, has been purified from the salivary glands of the short-tailed shrew Blarina brevicauda. Blarinasin is a 32-kDa N-glycosylated protease with isoelectric values ranging between 5.3 and 5.7, and an optimum pH of 8.5 for enzyme activity. The cloned blarinasin cDNA coded for a pre-pro-sequence and a mature peptide of 252 amino acids with a catalytic triad typical for serine proteases and 43.7–54.0% identity to other mammalian tissue kallikreins. Blarinasin preferentially hydrolysed Pro-Phe-Arg-4-methylcoumaryl-7-amide (MCA) and N-tert-butyloxycarbonyl-Val-Leu-Lys-MCA, and preferentially converted human high-molecular-weight kininogen (HK) to bradykinin. The activity of blarinasin was prominently inhibited by aprotinin (Ki=3.4 nM). A similar kallikrein-like protease, the lethal venom blarina toxin, has previously been purified from the salivary glands of the shrew Blarina and shows 67.9% identity to blarinasin. However, blarinasin was not toxic in mice. Blarinasin is a very abundant kallikrein-like protease and represents 70–75% of kallikrein-like enzymes in the salivary gland of B. brevicauda.
Type: article (author version)
URI: http://hdl.handle.net/2115/7398
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

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