NDLI: Expression, refolding and preliminary characterization of recombinant snake venom metalloproteinases: Implication for the hemorrhagic mechanism

Content Provider	Springer Nature Link
Author	Xiang, Kaijun Zou, Chunsen Zhu, Zhiqiang Teng, Maikun Niu, Liwen Liu, Jing
Copyright Year	2003
Abstract	Two cDNAs encoding hemorrhagic snake venom metalloproteinase acutolysin A and non-hemorrhagic metalloproteinase (BR) were cloned into the expression vector pET-22b, respectively, and the corresponding two recombinant proteins, A-22b and BR-22b, were produced in inclusion bodies in E. coli BL21(DE3). The recombinant proteins were then subjected to solubilization, purification and refolding in vitro. A-22b showed hemorrhagic activity but no detectable proteolytic activities toward fibrinogen and fibronectin. Natural acutolysin A had both hemorrhagic activity and proteolytic activity toward these substrates. BR-22b showed the proteolytic activities toward fibrinogen, but no hemorrhagic activity. In addition, two chimeric genes, C1 and C2, were constructed and cloned into pET-22b, and the corresponding recombinant proteins, C1–22b and C2–22b, were also expressed in inclusion bodies. C1-22b involved N-terminal 110 amino acids of BR and C-terminal 95 amino acids of acutolysin A, while C2–22b contained N-terminal 108 amino acids of acutolysin A and C-terminal 112 amino acids of BR. The biological activities of C2–22b and C1–22b were similar to those of A-22b and BR-22b, respectively. Our results suggested that N-terminal major subdomain of a snake venom metalloproteinase might play a key role in hemorrhagic activity and have an appreciable effect on the selectivity for protein substrates.
Starting Page	2055
Ending Page	2060
Page Count	6
File Format	PDF
ISSN	10016538
Journal	Chinese Science Bulletin
Volume Number	48
Issue Number	19
e-ISSN	18619541
Language	English
Publisher	Science in China Press
Publisher Date	2003-01-01
Publisher Place	Beijing
Access Restriction	Subscribed
Subject Keyword	snake venom metalloproteinase expression refolding hemorrhagic activity Science Life Sciences Physics Chemistry/Food Science Earth Sciences Engineering
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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