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- W2020143404 abstract "The likelihood that surface-induced blood coagulation results from specific protein-material interactions has led to a study of the conformation of adsorbed blood proteins. Infrared difference spectroscopy was used to determine the bound fraction, i.e., the fraction of carbonyl groups of an adsorbed molecule directly interacting with the surface, of serum albumin, prothrombin, and fibrinogen in situ. Measurements were carried out on individual proteins as a function of the amount adsorbed, time of absorption, pD, and ionic strength using a silica surface. The results obtained for serum albumin and prothrombin indicate that the internal bonding of these globular proteins is sufficient to prevent changes in the structure while adsorbed, even at low surface population. The bound fraction of fibrinogen increases with increasing adsorbance, suggesting possible interfacial aggregation. The conformation of all three proteins was found to be independent of the time of adsorption, although major differences in the rates of adsorption were observed. Studies of cross-linked and denatured serum albumin have provided information on the conformational changes concomitant with adsorption of the native protein. Qualitatively, such changes, if they occur, are small. This conclusion is supported by computer simulation studies of lysozyme adsorption. Studies of the effect of pD and ionic strength on the adsorbance and bound fraction of serum albumin show that caution must be exercised when identifying the plateau adsorbance of a protein isotherm with a close-packed monolayer." @default.
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- W2020143404 date "1974-01-01" @default.
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- W2020143404 title "The conformation of adsorbed blood proteins by infrared bound fraction measurements" @default.
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- W2020143404 doi "https://doi.org/10.1016/0021-9797(74)90036-8" @default.
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