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Purification and characterization of human nucleolar phosphoprotein 140 expressed in Escherichia coli

Title
Purification and characterization of human nucleolar phosphoprotein 140 expressed in Escherichia coli
Authors
Kim Y.-K.Jin Y.Vukoti K.M.Park J.K.Kim E.E.Lee K.-J.Yu Y.G.
Ewha Authors
이공주
SCOPUS Author ID
이공주scopus
Issue Date
2003
Journal Title
Protein Expression and Purification
ISSN
1046-5928JCR Link
Citation
vol. 31, no. 2, pp. 260 - 264
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Human nucleolar phosphoprotein 140, hNopp140, is one of the most highly phosphorylated mammalian proteins, which is involved in the biogenesis of nucleolus. It regulates the transcription of rDNA and has a tendency to bind to doxorubicin, which is widely used as an anti-cancer drug. The biochemical and biophysical property of hNopp140 has not been reported due to the fact that it is rather difficult to obtain protein in large enough quantity. In this paper, we report the cloning and overexpression of the soluble form of hNopp140 in Escherichia coli. The protein was purified to more than 90% homogeneity using hydroxyapatite and ion exchange chromatography. The purified protein can be extensively phosphorylated by casein kinase II and oligomerized into an insoluble aggregate in the presence of magnesium, carbonate, and fluoride ions. © 2003 Elsevier Inc. All rights reserved.
DOI
10.1016/S1046-5928(03)00194-3
Appears in Collections:
약학대학 > 약학과 > Journal papers
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