Studies of conformation change for interaction of lactoferrin and ferric ions by dual polarization interferometry (DPI).

碩士 === 淡江大學 === 生命科學研究所碩士班 === 93 === In this study, we use the dual polarization interfereometry (DPI) to measure the difference of lactoferrin protein after or before treated by iron ion. The parameters of conformation change of lactoferrin, surface concentration, thickness change and density on c...

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Bibliographic Details
Main Authors: Rung-Shin Wu, 吳榮信
Other Authors: 李世元
Format: Others
Language:zh-TW
Published: 2005
Online Access:http://ndltd.ncl.edu.tw/handle/30087184144072843044
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Summary:碩士 === 淡江大學 === 生命科學研究所碩士班 === 93 === In this study, we use the dual polarization interfereometry (DPI) to measure the difference of lactoferrin protein after or before treated by iron ion. The parameters of conformation change of lactoferrin, surface concentration, thickness change and density on chip can be determined by Maxwell methods. We also show the relationship of conformation change of lactoferrin proteins with the iron ion concentrations. When iron ion is dissociated from lactoferrin, conformation change of lactoferrin on DPI chip is thickness decrease and density increase, and when iron ion is associated from lactoferrin, conformation change of lactoferrin on DPI chip is thickness increase and density decrease. This results may be correlated with non-specific immobilization. When iron ion concentrations is 48.6~121.5 μM, the association between iron ion and lactoferrin will be saturated. The dynamic parameters of lactoferrin bind to iron ion can be determined by the molecule dynamic model.