Chen J, Andrade J D, VanWagenen R A
Biomaterials. 1985 Jul;6(4):231-6. doi: 10.1016/0142-9612(85)90018-3.
The adsorption of deoxyhaemoglobin (deoxyHb) and oxyhaemoglobin (oxyHb) was determined on clean glass, n-pentyl triethoxysilane (NPS)-treated glass, polystyrene (PS), and a polyetherurethane (PEU). The adsorbed amounts range from 0.1 to 0.6 micrograms/cm2 for oxyHb and from 0.3 to 0.7 micrograms/cm2 for deoxyHb. DeoxyHb adsorbs onto all these surfaces more than oxyHb. The more hydrophobic the surface, the more adsorption of both deoxy and oxyHb forms. These results suggest the oxyHb and deoxyHb interact differently with the surfaces studied. It is likely that the surface hydrophobicity of Hb plays a major role in Hb adsorption onto surfaces; the deoxyHb surface is more hydrophobic than the oxyHb surface. The binding sites for Hb adsorption may include the clefts between alpha 1, beta 1. A surface-induced dimerization mechanism is proposed to explain the adsorption of oxyHb.
测定了脱氧血红蛋白(deoxyHb)和氧合血红蛋白(oxyHb)在清洁玻璃、正戊基三乙氧基硅烷(NPS)处理过的玻璃、聚苯乙烯(PS)和聚醚聚氨酯(PEU)上的吸附情况。氧合血红蛋白的吸附量范围为0.1至0.6微克/平方厘米,脱氧血红蛋白的吸附量范围为0.3至0.7微克/平方厘米。脱氧血红蛋白在所有这些表面上的吸附量都比氧合血红蛋白多。表面疏水性越强,脱氧血红蛋白和氧合血红蛋白两种形式的吸附量就越大。这些结果表明,氧合血红蛋白和脱氧血红蛋白与所研究的表面相互作用方式不同。血红蛋白的表面疏水性很可能在其吸附到表面的过程中起主要作用;脱氧血红蛋白的表面比氧合血红蛋白的表面疏水性更强。血红蛋白吸附的结合位点可能包括α1、β1之间的裂隙。提出了一种表面诱导二聚化机制来解释氧合血红蛋白的吸附。