Green F A
Immunol Commun. 1982;11(1):25-32. doi: 10.3109/08820138209050721.
The extent of binding of anti-D antibody to intact RH (D) positive human erythrocytes at -2.5 degrees was approximately one-third that at 3- degrees. An Arrhenius plot of the temperature dependence of antibody binding showed a clear and reproducible discontinuity at approximately 6-8 degrees. Phospholipase A2 digestion of the intact erythrocytes resulted in a diminution of exclusively phosphatidylcholine (PC) from the membrane, and an approximately parallel loss of Rh antigen activity at 37 degrees to about 50% of the original. An Arrhenius plot showed no change in the temperature dependence below 6-8 degrees but significant diminution above that point suggesting that the outer membrane PC is involved in Rh (D) antigen activity manifested above that temperature.
在-2.5℃时，抗-D抗体与完整的RH（D）阳性人红细胞的结合程度约为3℃时的三分之一。抗体结合的温度依赖性的阿累尼乌斯图在约6-8℃处显示出明显且可重复的不连续性。完整红细胞经磷脂酶A2消化后，膜中仅磷脂酰胆碱（PC）减少，且在37℃时Rh抗原活性大约平行丧失至原来的50%。阿累尼乌斯图显示，在6-8℃以下温度依赖性无变化，但在该温度以上显著降低，这表明外膜PC参与了在该温度以上表现出的Rh（D）抗原活性。
