Heintz N H, Howard P L
Department of Pathology, University of Vermont, College of Medicine, Burlington 05405.
Am J Hematol. 1989 Jan;30(1):1-3. doi: 10.1002/ajh.2830300102.
Hemoglobin Casper is characterized by the substitution of cytidine for thymidine in condon 106 of the beta globin gene. This substitution results in the creation of a new restriction site for Msp I but not for the isoschizimer Hpa II. The restriction pattern following digestion with Msp I reveals a 9.9-kb fragment not seen in normal individuals or following digestion of Casper DNA with Hpa II. This finding confirms the predicted base mutation and indicates that the cytidine in the newly acquired CpG site is methylated.
血红蛋白卡斯珀的特征是β珠蛋白基因第106密码子中的胞嘧啶被胸腺嘧啶取代。这种取代导致产生了一个新的Msp I酶切位点，但没有产生同裂酶Hpa II的酶切位点。用Msp I酶消化后的酶切图谱显示出一个9.9 kb的片段，在正常个体中或用Hpa II酶消化卡斯珀DNA后都看不到这个片段。这一发现证实了预测的碱基突变，并表明新获得的CpG位点中的胞嘧啶是甲基化的。
