ISSN:
0021-9304
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
,
Technology
Notes:
A technique using 125-I-labeled proteins was employed to study static adsorption properties and slow exchange and desorption processes of human albumin in contact with synthetic hydroxyapatite beads. With the aid of a thermostated “minicolumn,” the adsorption isotherm was obtained during a so-called multiadsorption process, and could be described by a Langmuir adsorption model (K = 1.10 × 1010 cm3 · mol-1). All kinetic desorption and exchange experiments could be fitted by a simple exponential function of time. No influence of long-term interfacial residence times on characteristic relaxation times or percentage of desorbed or exchanged proteins could be detected in the present system. On the other hand, as compared to the low surface coverage domain, the small percentage of desorbable and high percentage of exchangeable molecules in the adsorption plateau domain was attributed to a bimolecular exchange process.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jbm.820231204
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