Costello A J, Marshall W E, Omachi A, Henderson T O
Biochim Biophys Acta. 1977 Apr 25;491(2):469-72. doi: 10.1016/0005-2795(77)90289-6.
The addition of 3 mM hemoglobin to 1-10 mM ATP solutions at pH 6.75 resulted in a linear relationship between the change in chemical shift (deltadelta) of the gamma-phosphate of ATP and the percent ATP bound to hemoglobin. The data points obtained with oxyhemoglobin and deoxyhemoglobin fell on the same straight line. In the presence of 3 mM Mg2+, the delta delta decreased curvilinearly as the percent ATP bound was raised. In this case, the percent ATP bound to deoxyhemoglobin was greater than to oxyhemoglobin at the same delta delta value, indicating that the extra ATP binding occurs through groups other than phosphate.
在pH 6.75条件下,向1 - 10 mM的ATP溶液中添加3 mM血红蛋白,导致ATP的γ-磷酸化学位移变化(δδ)与结合到血红蛋白上的ATP百分比之间呈线性关系。用氧合血红蛋白和脱氧血红蛋白获得的数据点落在同一条直线上。在存在3 mM Mg2+的情况下,随着结合的ATP百分比升高,δδ呈曲线下降。在这种情况下,在相同的δδ值下,结合到脱氧血红蛋白上的ATP百分比大于结合到氧合血红蛋白上的百分比,表明额外的ATP结合是通过磷酸以外的基团发生的。