Ochoa J L, Kristiansen T, Påhlman S
Biochim Biophys Acta. 1979 Mar 27;577(1):102-9. doi: 10.1016/0005-2795(79)90011-4.
The hydrophobicity of Concanavalin A has been estimated by its tendency to adsorb to hydrophobic adsorbents. Experiments varying temperature, salt concentration and hydrophobicity of the absorbent were consistent with accepted criteria of hydrophobic interaction between biomolecules and hydrophobic ligands. The biological significance of the hydrophobic character of Concanavalin A is also discussed.
伴刀豆球蛋白A的疏水性已通过其吸附到疏水吸附剂上的倾向来估算。改变温度、盐浓度和吸附剂疏水性的实验与生物分子和疏水配体之间疏水相互作用的公认标准一致。本文还讨论了伴刀豆球蛋白A疏水特性的生物学意义。