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作 者:CHEN Yong-li MAO Hai-bin ZHANG Xiu-fang GONG Yan-dao ZHAO Nan-ming 陈永丽;毛海滨;张秀芳;公衍道;赵南明(Department of Biological Science and Biotechnology,State Key Laboratory of Biomembrane and Membrane Biotechnology,Tsinghua University,Beijing 100084)
出 处:《Chinese Physics Letters》1999年第6期431-433,共3页中国物理快报(英文版)
基 金:Supported by the National Natural Science Foundation of China under Grant No.59493208.
摘 要:The increase of the protein transition enthalpy upon adsorption onto biomedical material surfaces was observed by measuringthe differential scanning calorimetry(DSC)traces of bovine fibrinogen adsorbed onto a hydroxyapatite surface.The mechanism causing the transition enthalpy increase upon adsorption was clariHed by using DSC measurements of bovine fibrinogen for different ionic strength and sodium dodecyl sulfate concentrations.The fesu7ts surest that the increased Hbrinogen transition enthalpy may be attributed to the electrostatic interactions between the carboxyl of the D domains and the calcium loci of hydroxyapatite,which may result in a more compact protein structure.
关 键 词:structure. surface. ENTHALPY
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