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Title: Cloning of habutobin cDNA and antithrombotic activity of recombinant protein

Abstract

The habutobin cDNA was cloned from total RNA extracted from venom glands of Trimeresurus flavoviridis (the habu snake). The conceptual translation of 1539 bp of habutobin cDNA consists of 236 amino acids and its molecular weight is 25.7 kDa. Histidine (His)-tagged recombinant habutobin fusion protein, pET-r-habutobin and AcNPV-r-habutobin, was purified by bacterial system and baculoviral system, respectively. After refolding pET-r-habutobin, there were two protein bands at about 32 kDa and 65 kDa, indicating that habutobin might be produced as a monomer protein and processed to form two concatenated protein. Purified AcNPV-r-habutobin dose-dependently increased fibrin forming activity and inhibited collagen-induced aggregation of rabbit washed platelets. Thus, AcNPV-r-habutobin produced by baculoviral system is very useful for study on structure-function relationship, which is necessary for developing an antithrombotic drug from habutobin.

Authors:
 [1]; ;  [1]
  1. 1st Department of Physiology, Unit of Physiological Science, School of Medicine, University of the Ryukyus, 207 Uehara, Nishihara, Okinawa 903-0215 (Japan)
Publication Date:
OSTI Identifier:
21032950
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 362; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2007.08.103; PII: S0006-291X(07)01787-1; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AGGLOMERATION; CLONING; COLLAGEN; DRUGS; FIBRIN; GLANDS; HISTIDINE; MOLECULAR WEIGHT; MONOMERS; RABBITS; RNA; SNAKES; STRUCTURE FUNCTIONS; THROMBIN; VENOMS

Citation Formats

Sunagawa, Masanori, Nakamura, Mariko, and Kosugi, Tadayoshi. Cloning of habutobin cDNA and antithrombotic activity of recombinant protein. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.08.103.
Sunagawa, Masanori, Nakamura, Mariko, & Kosugi, Tadayoshi. Cloning of habutobin cDNA and antithrombotic activity of recombinant protein. United States. https://doi.org/10.1016/j.bbrc.2007.08.103
Sunagawa, Masanori, Nakamura, Mariko, and Kosugi, Tadayoshi. 2007. "Cloning of habutobin cDNA and antithrombotic activity of recombinant protein". United States. https://doi.org/10.1016/j.bbrc.2007.08.103.
@article{osti_21032950,
title = {Cloning of habutobin cDNA and antithrombotic activity of recombinant protein},
author = {Sunagawa, Masanori and Nakamura, Mariko and Kosugi, Tadayoshi},
abstractNote = {The habutobin cDNA was cloned from total RNA extracted from venom glands of Trimeresurus flavoviridis (the habu snake). The conceptual translation of 1539 bp of habutobin cDNA consists of 236 amino acids and its molecular weight is 25.7 kDa. Histidine (His)-tagged recombinant habutobin fusion protein, pET-r-habutobin and AcNPV-r-habutobin, was purified by bacterial system and baculoviral system, respectively. After refolding pET-r-habutobin, there were two protein bands at about 32 kDa and 65 kDa, indicating that habutobin might be produced as a monomer protein and processed to form two concatenated protein. Purified AcNPV-r-habutobin dose-dependently increased fibrin forming activity and inhibited collagen-induced aggregation of rabbit washed platelets. Thus, AcNPV-r-habutobin produced by baculoviral system is very useful for study on structure-function relationship, which is necessary for developing an antithrombotic drug from habutobin.},
doi = {10.1016/j.bbrc.2007.08.103},
url = {https://www.osti.gov/biblio/21032950}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 4,
volume = 362,
place = {United States},
year = {Sat Nov 03 00:00:00 EDT 2007},
month = {Sat Nov 03 00:00:00 EDT 2007}
}