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Titolo:
Cloning and expression of catalytic domain of Abl protein tyrosine kinase gene in E-coli
Autore:
Qu, ZY; Zheng, S; Xu, B; Guo, CL; Xiao, P; Gu, HX;
Indirizzi:
Harbin Med Coll, Dept Microbiol, Harbin 150086, Peoples R China Harbin MedColl Harbin Peoples R China 150086 in 150086, Peoples R China Zhejiang Univ, Inst Canc, Hangzhou 310009, Peoples R China Zhejiang Univ Hangzhou Peoples R China 310009 ou 310009, Peoples R China
Titolo Testata:
PROGRESS IN NATURAL SCIENCE
fascicolo: 8, volume: 11, anno: 2001,
pagine: 637 - 640
SICI:
1002-0071(200108)11:8<637:CAEOCD>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIGNAL-TRANSDUCTION; INHIBITORS;
Keywords:
PTK; signal transduction; Abl; fusion protein expression; gene cloning;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
6
Recensione:
Indirizzi per estratti:
Indirizzo: Qu, ZY Harbin Med Coll, Dept Microbiol, Harbin 150086, Peoples R China Harbin Med Coll Harbin Peoples R China 150086 86, Peoples R China
Citazione:
Z.Y. Qu et al., "Cloning and expression of catalytic domain of Abl protein tyrosine kinase gene in E-coli", PROG NAT SC, 11(8), 2001, pp. 637-640

Abstract

Protein tyrosine kinases (PTKs) regulate cell proliferation, differentiation and are involved in signal transduction. Uncontrolled signaling from receptor tyrosine kinases to intracellular tyrosine kinases can lead to inflammatory responses and diseases such as cancer and atherosclerosis. Thus, inhibitors that block the activity of tyrosine kinases or the signaling pathways of PTKs activation could be assumed as the potential candidate for drug development. On this assumption, we cloned and expressed the Abl PTK gene in E. coli, and purified the PTK, which was used to screen the PTK inhibitors from the extracts of Chinese herbs. The catalytic domain sequence of PTK gene was amplified by PCR using the cDNA of ab1 from Abelson murine leukemia virus as template. The amplified fragment was then cloned into the GST-tagged expression vector pGEX2T. The recombinant plasmid was transformed intohost cell E. coli DH5 alpha and was induced to express PTK protein. The expression of the protein was detected using SDS-PAGE. The result showed thata specific protein was induced to express after 12 min induction, and reached peak level about 40% of the host total protein after 4 h induction. Themolecular weight of the fusion protein was about 58 kD. The purified GST-PTK fusion protein presented higher activity for tyrosine phosphorylation.

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Documento generato il 10/07/20 alle ore 12:53:09