ADSORPTION OF PROTEINS FROM PLASMA TO A SERIES OF HYDROPHILIC-HYDROPHOBIC CO-POLYMERS .1. ANALYSIS WITH THE INSITU RADIOIODINATION TECHNIQUE
ADSORPTION OF PROTEINS FROM PLASMA TO A SERIES OF HYDROPHILIC-HYDROPHOBIC CO-POLYMERS .1. ANALYSIS WITH THE INSITU RADIOIODINATION TECHNIQUE
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DOI：
10.1002/jbm.820150311
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发表时间：
1981-01-01
期刊：
影响因子：
--
通讯作者：
WEATHERSBY, PK
中科院分区：
文献类型：
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作者：
HORBETT, TA;WEATHERSBY, PK
蛋白质的吸附影响细胞与外来表面的相互作用，因此在确定植入物的生物相容性方面起着重要作用。以前的研究表明，不同的蛋白质对一个给定的聚合物的亲和力的差异，和纤维蛋白原的亲水性不同的一系列聚合物的亲和力的差异。这些研究表明，吸附到[牛]血浆聚合物上的蛋白质层组成可能存在差异。为了检验这一假设，从血浆中吸附到一系列亲水性不同的聚合物的蛋白质与碘谱技术进行了分析。将由辐射接枝技术制成的甲基丙烯酸羟乙酯和甲基丙烯酸乙酯的共聚物暴露于等离子体中0.5或150 min。将吸附的蛋白质碘化，用SDS [十二烷基硫酸钠]洗脱，并用聚丙烯酰胺凝胶电泳分离。纤维蛋白原，IG，血红蛋白和一个峰暂时归因于凝血酶原检测到的主要蛋白质。很少I被结合到吸附的白蛋白中，即使它是通过使用染料结合的单独实验存在的。与9种蛋白质中的每一种相关的总放射性的分数在表面之间显著而系统地变化。在血浆暴露0.5和150 min的聚合物上，蛋白质中的放射性分布非常不同。结果反映了聚合物上的吸附蛋白质层的组成差异和蛋白质在吸附状态下对标记试剂的可及性差异。吸附的蛋白质层的组织的差异可能在确定细胞表面受体是否可以与能够进一步刺激细胞的特定血浆蛋白质接触中起关键作用。
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 [bovine] 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 [sodium dodecyl sulfate] and separated with polyacrylamide gel electrophoresis. Fibrinogen, IG, hemoglobin and a peak tentatively ascribed to prothrombin were the major proteins detected. Very little I was incorporated into adsorbed albumin, even though it was present by a separate experiment using dye binding. The fraction of total radioactivity associated with each of 9 proteins varied 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.