Allen G
Biochem J. 1974 Mar;137(3):575-8. doi: 10.1042/bj1370575.
The extent of binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios was investigated by gel filtration. The weight ratio of bound sodium dodecyl sulphate to bovine serum albumin increases with the NaCl concentration, and, except at low salt concentrations, with the concentration of sodium dodecyl sulphate. In the presence of 1.0g of sodium dodecyl sulphate/l, the binding ratio varied from 1.0 (at 0.04m-Na(+)) to 2.2 (at 0.44m-Na(+)). In the presence of 0.24m-Na(+), the binding ratio increased with sodium dodecyl sulphate concentration, from 0.9 (0.2g of sodium dodecyl sulphate/l) to 2.0 (5g of sodium dodecyl sulphate/l), at 26 degrees C, in a dilute sodium phosphate buffer. No significant dependence of the binding ratio upon temperature in the range 26-45 degrees C was observed. These results differ from those of Reynolds & Tanford (1970a) obtained by equilibrium dialysis.
通过凝胶过滤法研究了在高结合率下十二烷基硫酸钠与牛血清白蛋白的结合程度。结合的十二烷基硫酸钠与牛血清白蛋白的重量比随氯化钠浓度增加而增加，并且除了在低盐浓度下，还随十二烷基硫酸钠浓度增加而增加。在每升含有1.0克十二烷基硫酸钠的情况下，结合率在0.04m - Na⁺时为1.0，在0.44m - Na⁺时为2.2。在26℃的稀磷酸钠缓冲液中，当存在0.24m - Na⁺时，结合率随十二烷基硫酸钠浓度增加，从每升0.2克十二烷基硫酸钠时的0.9增加到每升5克十二烷基硫酸钠时的2.0。在26 - 45℃范围内未观察到结合率对温度有显著依赖性。这些结果与雷诺兹和坦福德（1970a）通过平衡透析法得到的结果不同。
