Functional Difference between N Domain and C Domain of hEGF and hTGF-alpha

Autor: Yu, Yuan, Qian, Zhang, Pei-Yong, Huang, Yi-Fei, Wang, Qing-Wei, Zhou, Ren-Bao, Gan, Zai-Ping, Li
Rok vydání: 2002
Zdroj: Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica. 31(5)
ISSN: 0582-9879
Popis: By exchanging the N domain and C domain of hEGF and hTGF-alpha genes by PCR, two chimeras E-TGF(EGF(1-32)-TGF-alpha(34-50))and T-EGF(TGF-alpha(1-33)-EGF(33-53))were constructed. The wild and chimeric molecules were expressed in E.coli under phoA system. The expressed hEGF, hTGF-alpha and two chimeras were purified. The EGF receptor competitive binding affinity of the four molecules was hEGFhTGF-alpha and E-TGFT-EGF and the cell proliferation stimulating activity of them was hTGF-alpha and E-TGFT-EGFhEGF. The result suggests that the N domain of hEGF and hTGF-alpha may play a major role in receptor binding activity and C domain of them may be responsible for stimulating cell proliferation.
Databáze: OpenAIRE