On the adsorption of serum proteins on polymer membrane surfaces
A detailed study of the adsorption and desorption of bovine serum albumin, γ-globulin, and fibrinogen at physiological conditions on a series of polymer membranes, both cation exchangers and neutral, has been carried out. The results obtained indicate that adsorption takes place in two separate and...
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Published in | Journal of colloid and interface science Vol. 44; no. 2; pp. 221 - 241 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Elsevier Inc
01.01.1973
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Online Access | Get full text |
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Summary: | A detailed study of the adsorption and desorption of bovine serum albumin, γ-globulin, and fibrinogen at physiological conditions on a series of polymer membranes, both cation exchangers and neutral, has been carried out. The results obtained indicate that adsorption takes place in two separate and distinct ways simultaneously. Both types of adsorption are apparently Langmuir (monolayer) in type, taking place on separate membrane sites and are noninteracting. One type of adsorption is characterized as being relatively hydrophilic, exothermic, and easily reversible with a heat of adsorption in the neighborhood of −10 kcal/ mole. The other type of adsorption is apparently tightly bound, hydrophobic, and endothermic, with heats of adsorption ranging from ∼5 kcal/mole to ∼20 kcal/mole. |
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ISSN: | 0021-9797 1095-7103 |
DOI: | 10.1016/0021-9797(73)90215-4 |