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Title 

Expression, purification and characterization of soluble human thrombopoietin receptor from Escherichia coli

Authors 

Heung Rok ParkHa Na ImYoung Jun KangMyeong Hee YuHyo Jeong Hong

Publisher 

Springer Verlag (Germany)

Issue Date 

2000

Citation 

Biotechnology Letters, vol. 22, no. 20, pp. 1611-1617

Keywords 

inclusion bodiesprotein purificationreceptor domainthrombopoietincell receptorthrombopoietin receptorEscherichia colihumannonhuman

Abstract 

The extracellular domain (edMpl) of human thrombopoietin (TPO) receptor, c-Mpl was expressed in Escherichia coli by changing some nucleotides before and after the translation initiation codon. The mutations increased the expression by approx. 15-fold. The inclusion bodies were solubilized in 8 M guanidine-HCl under reducing conditions and refolded using a glutathione-redox system. The monomeric form of edMpl was purified to near homogeneity by two successive steps of ion-exchange chromatography using DEAE-Sephacel and Mono Q columns. The purified monomeric edMpl inhibited the TPO-dependent cell proliferation, suggesting that it was binding to TPO. Also, antisera raised against the edMpl bound specifically to the soluble receptor secreted by mammalian cells.

ISSN 

0141-5492

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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