Binding Constants for Terbium(Ⅲ) with Chicken Apoovotransferrin

高等学校化学研究 ›› 2001, Vol. 17 ›› Issue (1): 6-13.

Binding Constants for Terbium(Ⅲ) with Chicken Apoovotransferrin

YANG Bin-sheng, LI Ying-qi

Institute of Molecular Science, Shanxi University, Taiyuan 030006, P. R. China

收稿日期:1999-11-17 出版日期:2001-01-24 发布日期:2011-08-04
基金资助:
Supported by the National Natural Science Foundation of China(No.200710220), Natural Science Foundation of Shanxi Province(No.991013)and Shanxi Returned scholar Foundation.

Binding Constants for Terbium(Ⅲ) with Chicken Apoovotransferrin

YANG Bin-sheng, LI Ying-qi

Institute of Molecular Science, Shanxi University, Taiyuan 030006, P. R. China

Received:1999-11-17 Online:2001-01-24 Published:2011-08-04
Supported by:
Supported by the National Natural Science Foundation of China(No.200710220), Natural Science Foundation of Shanxi Province(No.991013)and Shanxi Returned scholar Foundation.

摘要/Abstract

摘要： The binding of Tb³⁺ to chicken apoovotransferrin was studied by monitoring the fluorescent intensity of Tb³⁺ at 549 nm. The conditional equilibrium constants for the complexation of Tb³⁺ by chicken apoovotransferrin in 0.1 mol/L hepes, at pH 7.4 and room temperature were measured. The successive macroscopic binding constants are lgK₁=9.08±0.12 and lgK₂=7.36±0.22. The molar fluorescence enhancement of Tb³⁺-apoovotransferrin complex is (2.06±0.14)×10⁴ mol^-1·L. The fluorescence quenching experiment and the titration of N-terminal monoferric ovotransferrin showed that Tb³⁺ has a preference for being bound to the N-terminal binding site of apoovotransferrin.

关键词: Terbium, Transferrin, Binding constant, Fluorescence

Abstract: The binding of Tb³⁺ to chicken apoovotransferrin was studied by monitoring the fluorescent intensity of Tb³⁺ at 549 nm. The conditional equilibrium constants for the complexation of Tb³⁺ by chicken apoovotransferrin in 0.1 mol/L hepes, at pH 7.4 and room temperature were measured. The successive macroscopic binding constants are lgK₁=9.08±0.12 and lgK₂=7.36±0.22. The molar fluorescence enhancement of Tb³⁺-apoovotransferrin complex is (2.06±0.14)×10⁴ mol^-1·L. The fluorescence quenching experiment and the titration of N-terminal monoferric ovotransferrin showed that Tb³⁺ has a preference for being bound to the N-terminal binding site of apoovotransferrin.

Key words: Terbium, Transferrin, Binding constant, Fluorescence

YANG Bin-sheng, LI Ying-qi. Binding Constants for Terbium(Ⅲ) with Chicken Apoovotransferrin[J]. 高等学校化学研究, 2001, 17(1): 6-13.

YANG Bin-sheng, LI Ying-qi. Binding Constants for Terbium(Ⅲ) with Chicken Apoovotransferrin[J]. Chemical Research in Chinese Universities, 2001, 17(1): 6-13.

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Binding Constants for Terbium(Ⅲ) with Chicken Apoovotransferrin

Binding Constants for Terbium(Ⅲ) with Chicken Apoovotransferrin

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