Adsorption of proteins from plasma to a series of hydrophilic-hydrophobic copolymers. I. Analysis with the in situ radioiodination technique

Journal Article · Fri May 01 04:00:00 EDT 1981 · J. Biomed. Mater. Res.; (United States)

DOI:https://doi.org/10.1002/jbm.820150311· OSTI ID:6525096

Horbett, T A; Weathersby, P K

The adsorption of proteins affects cellular interactions with foreign surfaces and thus plays an important role in determining the biocompatibility of implants. Previous studies have indicated differences in the affinity of various proteins for a given polymer, and differences in the affinity of fibrinogen for a series of polymers varying in hydrophilicity. These studies suggest that differences in the composition of the protein layer adsorbed to polymers from plasma might exist. To examine this hypothesis, the proteins adsorbed from plasma to a series of polymers varying in hydrophilicity were analyzed with the iodogram technique. Copolymers of hydroxyethyl methacrylate and ethyl methacrylate made by the radiation grafting technique were exposed to plasma for 0.5 or 150 min. The adsorbed proteins were iodinated, eluted with SDS, and separated with polyacrylamide gel electrophoresis. Fibrinogen, immunoglobulin G, hemoglobin, and a peak tentatively ascribed to prothrombin were the major proteins detected. Very little iodine was incorporated into adsorbed albumin, even though it was shown to be present by a separate experiment using dye binding. The fraction of total radioactivity associated with each of nine proteins was found to vary markedly and systematically among the surfaces. The distribution of radioactivity into the proteins was very different on 0.5 and 150-min plasma exposed polymers. The results reflect both compositional differences in the adsorbed protein layer on the polymers and differences in the accessibility of proteins to the labeling reagent in the adsorbed state. Differences in the organization of the adsorbed protein layer may play a key role in determining whether cell surface receptors can come in contact with the specific plasma protein able to further stimulate the cell.

• Research Organization: Department of Chemical Engineering, University of Washington, Seattle
• OSTI ID: 6525096
• Journal Information: J. Biomed. Mater. Res.; (United States), Journal Name: J. Biomed. Mater. Res.; (United States) Vol. 15:3; ISSN JBMRB
• Country of Publication: United States
• Language: English

Related Subjects

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59 BASIC BIOLOGICAL SCIENCES
62 RADIOLOGY AND NUCLEAR MEDICINE
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL MATERIALS
BIOLOGICAL PATHWAYS
BLOOD
BLOOD COAGULATION FACTORS
BLOOD PLASMA
BODY FLUIDS
CARBOXYLIC ACIDS
CHEMICAL PREPARATION
COAGULANTS
DRUGS
FIBRINOGEN
GLOBIN
GLOBULINS
GRAFT-HOST REACTION
HEMATOLOGIC AGENTS
HEMOGLOBIN
HEMOSTATICS
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
IMMUNOGLOBULINS
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
MATERIALS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PIGMENTS
POLYMERS
PORPHYRINS
PROTEINS
PROTHROMBIN
REACTION KINETICS
SYNTHESIS
TRANSPLANTS