van Holde K E, Miller K I
Biochemistry. 1985 Aug 13;24(17):4577-82. doi: 10.1021/bi00338a014.
The equilibria between the native (decameric) Octopus hemocyanin and its subunits were studied by analytical sedimentation. Equilibrium is obtained slowly, but the reaction is thermodynamically reversible. The mass action law for a monomer-decamer reaction is obeyed. The reassociated hemocyanin is virtually identical in its sedimentation behavior and oxygen binding with the native protein. The association-dissociation equilibria are mediated by cations; Mg2+, Ca2+, Na+, and H+ are all effective in stabilizing the decameric form at appropriate concentrations. About three to four cations per monomer must be bound for association to occur. Under some conditions, dimers of the subunits can be observed, but formation of this dimer does not depend on cation concentration, and it does not appear to be an obligate intermediate in the association to decamer.
通过分析沉降法研究了天然（十聚体）章鱼血蓝蛋白与其亚基之间的平衡。平衡状态建立缓慢，但该反应在热力学上是可逆的。单体 - 十聚体反应遵循质量作用定律。重新缔合的血蓝蛋白在沉降行为和氧结合方面与天然蛋白几乎相同。缔合 - 解离平衡由阳离子介导；Mg2 +、Ca2 +、Na +和H +在适当浓度下均能有效稳定十聚体形式。每个单体必须结合大约三到四个阳离子才能发生缔合。在某些条件下，可以观察到亚基的二聚体，但这种二聚体的形成不依赖于阳离子浓度，并且它似乎不是缔合形成十聚体过程中的必需中间体。
