Mannhalter C, Schiffman S
Thromb Haemost. 1982 Jun 28;47(3):214-7.
Blood coagulation factors XI and XIa possess binding site(s) for glass and plastics, located in the heavy chain of the molecule. To elucidate the nature of binding, adsorption and desorption properties of factor XI and XIa to different surfaces have been studied. Desorption experiments with high salt (2.4 M NaC1) suggest participation of ionic forces in the binding to glass. This is consistent with the decreased adsorption of factor XI (pI-9.0) to glass with increasing pH. The non-ionic detergent Triton X-100, which splits hydrophobic bonds, desorbs factor XI very well from plastics and partially from glass. The anionic detergent SDS, which will split hydrophobic as well as ionic bonds, is the most effective agent tested for the elution of factor XI from glass. We, therefore infer, that the binding of factor XI to glass is the combined effect of ionic and hydrophobic binding, whereas the adsorption of factor XI to plastics is primarily hydrophobic.
血液凝固因子XI和XIa在分子的重链上拥有与玻璃和塑料的结合位点。为了阐明结合的本质,已经研究了因子XI和XIa对不同表面的吸附和解吸特性。用高盐(2.4M NaCl)进行的解吸实验表明离子力参与了与玻璃的结合。这与随着pH值升高因子XI(pI-9.0)对玻璃的吸附减少是一致的。能破坏疏水键的非离子去污剂Triton X-100能很好地使因子XI从塑料上解吸,部分地从玻璃上解吸。能破坏疏水键和离子键的阴离子去污剂SDS是从玻璃上洗脱因子XI测试过的最有效的试剂。因此,我们推断,因子XI与玻璃的结合是离子结合和疏水结合的综合作用,而因子XI对塑料的吸附主要是疏水作用。