Phosphoprotein partitioning in metal-affinity aqueous two-phase systems and prediction of partitioning behavior = 금속 친화성 액 이상분계 시스템에서 phosphoprotein 분배 및 분배예측

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Title
Phosphoprotein partitioning in metal-affinity aqueous two-phase systems and prediction of partitioning behavior = 금속 친화성 액 이상분계 시스템에서 phosphoprotein 분배 및 분배예측
Author(s)
Bong Hyun Chung
Bibliographic Citation
Korean Journal of Biotechnology and Bioengineering, vol. 9, no. 3, pp. 279-286
Publication Year
1994
Abstract
A mather latical model has been derived and used to describe phosphoprotein partitioning in Fe(III) IDA-PEG/( extran two-phase systems. This model includes the inhibitory effects of hydrogen and hydroxyl io:. concentrations on protein partitioning. For aqueous two-phase partitioning experiments, the Al and A2 subcomponents of ovalbumin carrying two and one surface phosphoryl group(s) were purified usii g an immobilized metal ion affinity chromatography (IMAC). The ratio of partition coefficients in the presence and absence of Fe(III)IDA-PEG, K/Ko, increased in the pH range of 3.0 to 5.0 due to deprt tonation of the second oxygen of the phosphoryl group, and above pH 5.0 declined steeply by the inhit tory binding of hydroxyl ions to the metal ion. This partitioning behavior was well-described by t le mathematical model. The binding constants for formation of the complex between the phosphoryl 혼 roup and the Fe(III)IDA-PEG were found to be 6.1 x 103 and 2.3 X104 M_l in the top and bottom chases, respectively. These values are 3-5 times those for interaction of Cu(II)IDA-PEG with a single surf ace-accessible histidine.
ISSN
1225-7117
Publisher
Korea Soc-Assoc-Inst
Type
Article
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1. Journal Articles > Journal Articles
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