Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/11980
Title: Construction of three different recombinant scorpion fusion proteins with bifunctional activity
Authors: Cui, Y
Guo, G L
Liu, Y F
Mao, Y Z
Zhang, R
Wu, C F
Zhang, J H
Keywords: Antitumor-analgesic peptide
Difunctionality
<i>E. coli</i>
Fusion protein
Linker
Recombinant expression
Issue Date: Jun-2011
Publisher: NISCAIR-CSIR, India
Abstract: This is the first report of three different fusion proteins with an antitumor-analgesic peptide obtained from Chinese scorpion <i style="">Buthus martensii </i>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 <i>E. coli</i> 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.
Description: 141-147
URI: http://hdl.handle.net/123456789/11980
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.48(3) [June 2011]

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