Functional characterization of recombinant batroxobin, a snake venom thrombin-like enzyme, expressed from Pichia pastoris

Weon Kyoo You; Won Seok Choi; You Seok Koh; Hang Cheol Shin; Yangsoo Jang; Kwang Hoe Chung

doi:10.1016/j.febslet.2004.06.060

Functional characterization of recombinant batroxobin, a snake venom thrombin-like enzyme, expressed from Pichia pastoris

Weon Kyoo You, Won Seok Choi, You Seok Koh, Hang Cheol Shin, Yangsoo Jang, Kwang Hoe Chung

Department of Internal Medicine

Research output: Contribution to journal › Article › peer-review

45 Citations (Scopus)

Abstract

A thrombin-like enzyme of Bothrops atrox moojeni venom, batroxobin, specifically cleaves fibrinogen α chain, resulting in the formation of non-crosslinked fibrin clots. The cDNA encoding batroxobin was cloned, expressed in Pichia pastoris and the molecular function of purified recombinant protein was also characterized. The recombinant batroxobin had an apparent molecular weight of 33 kDa by SDS-PAGE analysis and biochemical activities similar to those of native batroxobin. The purified recombinant protein strongly converted fibrinogen into fibrin clot in vitro, and shortened bleeding time and whole blood coagulation time in vivo. However, it did not make any considerable alterations on other blood coagulation factors. Several lines of experimental evidence in this study suggest that the recombinant batroxobin is a potent pro-coagulant agent.

Original language	English
Pages (from-to)	67-73
Number of pages	7
Journal	FEBS Letters
Volume	571
Issue number	1-3
DOIs	https://doi.org/10.1016/j.febslet.2004.06.060
Publication status	Published - 2004 Jul 30

Bibliographical note

Funding Information:
This study was supported in part by the grant from the Korean Ministry of Commerce, Industry, and Energy and by the BK21 project from the Korean Ministry of Education and Human Resources Development. We thank Dr. Ikuo Yamashina for his helpful support and kind donation of the full-length cDNA of batroxobin.

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/j.febslet.2004.06.060

Cite this

@article{821a302e7e1b4f708527275ba8a5b0e0,

title = "Functional characterization of recombinant batroxobin, a snake venom thrombin-like enzyme, expressed from Pichia pastoris",

abstract = "A thrombin-like enzyme of Bothrops atrox moojeni venom, batroxobin, specifically cleaves fibrinogen α chain, resulting in the formation of non-crosslinked fibrin clots. The cDNA encoding batroxobin was cloned, expressed in Pichia pastoris and the molecular function of purified recombinant protein was also characterized. The recombinant batroxobin had an apparent molecular weight of 33 kDa by SDS-PAGE analysis and biochemical activities similar to those of native batroxobin. The purified recombinant protein strongly converted fibrinogen into fibrin clot in vitro, and shortened bleeding time and whole blood coagulation time in vivo. However, it did not make any considerable alterations on other blood coagulation factors. Several lines of experimental evidence in this study suggest that the recombinant batroxobin is a potent pro-coagulant agent.",

author = "You, {Weon Kyoo} and Choi, {Won Seok} and Koh, {You Seok} and Shin, {Hang Cheol} and Yangsoo Jang and Chung, {Kwang Hoe}",

note = "Funding Information: This study was supported in part by the grant from the Korean Ministry of Commerce, Industry, and Energy and by the BK21 project from the Korean Ministry of Education and Human Resources Development. We thank Dr. Ikuo Yamashina for his helpful support and kind donation of the full-length cDNA of batroxobin.",

year = "2004",

month = jul,

day = "30",

doi = "10.1016/j.febslet.2004.06.060",

language = "English",

volume = "571",

pages = "67--73",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1-3",

}

TY - JOUR

T1 - Functional characterization of recombinant batroxobin, a snake venom thrombin-like enzyme, expressed from Pichia pastoris

AU - You, Weon Kyoo

AU - Choi, Won Seok

AU - Koh, You Seok

AU - Shin, Hang Cheol

AU - Jang, Yangsoo

AU - Chung, Kwang Hoe

N1 - Funding Information: This study was supported in part by the grant from the Korean Ministry of Commerce, Industry, and Energy and by the BK21 project from the Korean Ministry of Education and Human Resources Development. We thank Dr. Ikuo Yamashina for his helpful support and kind donation of the full-length cDNA of batroxobin.

PY - 2004/7/30

Y1 - 2004/7/30

N2 - A thrombin-like enzyme of Bothrops atrox moojeni venom, batroxobin, specifically cleaves fibrinogen α chain, resulting in the formation of non-crosslinked fibrin clots. The cDNA encoding batroxobin was cloned, expressed in Pichia pastoris and the molecular function of purified recombinant protein was also characterized. The recombinant batroxobin had an apparent molecular weight of 33 kDa by SDS-PAGE analysis and biochemical activities similar to those of native batroxobin. The purified recombinant protein strongly converted fibrinogen into fibrin clot in vitro, and shortened bleeding time and whole blood coagulation time in vivo. However, it did not make any considerable alterations on other blood coagulation factors. Several lines of experimental evidence in this study suggest that the recombinant batroxobin is a potent pro-coagulant agent.

AB - A thrombin-like enzyme of Bothrops atrox moojeni venom, batroxobin, specifically cleaves fibrinogen α chain, resulting in the formation of non-crosslinked fibrin clots. The cDNA encoding batroxobin was cloned, expressed in Pichia pastoris and the molecular function of purified recombinant protein was also characterized. The recombinant batroxobin had an apparent molecular weight of 33 kDa by SDS-PAGE analysis and biochemical activities similar to those of native batroxobin. The purified recombinant protein strongly converted fibrinogen into fibrin clot in vitro, and shortened bleeding time and whole blood coagulation time in vivo. However, it did not make any considerable alterations on other blood coagulation factors. Several lines of experimental evidence in this study suggest that the recombinant batroxobin is a potent pro-coagulant agent.

UR - http://www.scopus.com/inward/record.url?scp=3342934815&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=3342934815&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2004.06.060

DO - 10.1016/j.febslet.2004.06.060

M3 - Article

C2 - 15280019

AN - SCOPUS:3342934815

SN - 0014-5793

VL - 571

SP - 67

EP - 73

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Functional characterization of recombinant batroxobin, a snake venom thrombin-like enzyme, expressed from Pichia pastoris

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this