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Construction of three different recombinant scorpion fusion proteins with bifunctional activity

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Title Construction of three different recombinant scorpion fusion proteins with bifunctional activity
 
Creator Cui, Y
Guo, G L
Liu, Y F
Mao, Y Z
Zhang, R
Wu, C F
Zhang, J H
 
Subject Antitumor-analgesic peptide
Difunctionality
E. coli
Fusion protein
Linker
Recombinant expression
 
Description 141-147
This is the first report of three different
fusion proteins with an antitumor-analgesic peptide obtained from Chinese scorpion
Buthus martensii Karsch (BmKAGAP). The fusion
proteins were constructed in the form of chimeric toxins, aiming to obtain
bifunctional analgesic and antitumor activity. The fusion proteins consisted of
luteinizing hormone-releasing hormone (LHRH), three different types of flexible linkers (L1,
Ser-Ser-His-His-His-His-His-His-Ser-Ser-Gly-Leu-Val-Pro-Arg-Gly-Ser-His-Met;
L2, Gly-Gly-Gly-Ser-Gly-Gly-Gly-Ser; L3,
Ser-Gly-Gly-Ser-Gly-Gly-Ser-Gly-Gly-Gly-Ser-Ser-Gly-Gly-Ser-Gly-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Gly-Ser), and BmKAGAP.
The genes coding three fusion proteins were cloned and expressed in E. coli in soluble form. Following two successive column
chromatographic separations, purified fusion proteins were obtained. These
fusion proteins exhibited analgesic activity in mice and were cytotoxic to a
hepatocellular carcinoma cell line Hep3B.
 
Date 2011-06-16T09:09:08Z
2011-06-16T09:09:08Z
2011-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/11980
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.48(3) [June 2011]