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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
| 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)
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Submitter: 大舘 智志
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