Authors:
X. Li Hunan University of Science and Technology School of Chemistry and Chemical Engineering Xiangtan 411201 People’s Republic of China

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C. Wang Wuhan University College of Chemistry and Molecular Science Wuhan 430072 People’s Republic of China

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J. Li Wuhan University College of Chemistry and Molecular Science Wuhan 430072 People’s Republic of China

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Z. Wang Wuhan University College of Chemistry and Molecular Science Wuhan 430072 People’s Republic of China

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Abstract  

The interactions of lanthanide ions (Ln3+) with bovine serum albumin (BSA) under mimetic physiological conditions (310.15 K, pH 6.7, 0.1MNaCl) were studied by microcalorimetry. For the first time, based on Two Sets of Independent Sites Model, molar enthalpies (ΔrHm1, ΔrHm2) and coordination number (n1, n2) of the two sets of binding sites with different affinity were obtained directly from the microcalorimetric results. It was shown that the interactions are endothermic and entropy-driving processes. By combining with fluorescence spectroscopy, other thermodynamic parameters (ΔrGm1, ΔrSm1) were determined for high-affinity specific sites.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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