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[Untitled]
- Source :
- Biotechnology Letters. 22:1611-1617
- Publication Year :
- 2000
- Publisher :
- Springer Science and Business Media LLC, 2000.
-
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.
- Subjects :
- Thrombopoietin receptor
food and beverages
Bioengineering
General Medicine
Biology
medicine.disease_cause
Applied Microbiology and Biotechnology
Molecular biology
Inclusion bodies
law.invention
Biochemistry
law
Protein purification
medicine
Recombinant DNA
Extracellular
Receptor
Escherichia coli
Thrombopoietin
Biotechnology
Subjects
Details
- ISSN :
- 01415492
- Volume :
- 22
- Database :
- OpenAIRE
- Journal :
- Biotechnology Letters
- Accession number :
- edsair.doi...........f500ced791f35c9d1730b90ca5ca0fe6