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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

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1437-4315
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Volume 386, Issue 2 (Feb 2005)

Issues

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

Masaki Kita
  • Research Center for Materials Science, Nagoya University, Furo-cho, Chikusa, Nagoya 464-8602, Japan
/ Yuushi Okumura
  • Institute for Enzyme Research, The University of Tokushima, Kuramoto-Cho 3-18-15, Tokushima 770-8503, Japan
/ Satoshi D. Ohdachi
  • Institute of Low Temperature Science, Hokkaido University, Kita-19 Nishi-8, Kita-ku, Sapporo 060-0819, Japan
/ Yuichi Oba
  • Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa, Nagoya 464-8601, Japan
/ Michiyasu Yoshikuni
  • Laboratory of Reproductive Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji, Okazaki 444-8585, Japan
/ Yasuo Nakamura
  • Institute for Enzyme Research, The University of Tokushima, Kuramoto-Cho 3-18-15, Tokushima 770-8503, Japan
/ Hiroshi Kido
  • Institute for Enzyme Research, The University of Tokushima, Kuramoto-Cho 3-18-15, Tokushima 770-8503, Japan
/ Daisuke Uemura
  • Graduate School of Science, Nagoya University, Furo-cho, Chikusa, Nagoya 464-8602, Japan
Published Online: 2005-06-01 | DOI: https://doi.org/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 (K i=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.

Keywords: amino acid sequence analysis; blarina toxin; blarinasin; salivary glands; short-tailed shrew; tissue kallikrein

About the article

Corresponding author


Received: October 11, 2004

Accepted: December 15, 2004

Published Online: 2005-06-01

Published in Print: 2005-02-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2005.022.

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