Johnson C A, Chung K S, McGrath K M, Bean P E, Roberts H R
Br J Haematol. 1980 Mar;44(3):461-9. doi: 10.1111/j.1365-2141.1980.tb05916.x.
An 18-month-old child, who had no evidence of liver disease, malabsorption, or chronic ingestion of coumarin compounds, was found to have plasma deficiencies of factors II, VII, IX and X. Assays for factor II and X by immunological techniques (antibody neutralization and immunoelectrophoresis) revealed normal or elevated antigenic activity of these factors, suggesting the presence of abnormal protein variants in the patient's plasma. On two-dimensional immunoelectrophoresis of the patient's plasma in calcium, a normal and an abnormal population of prothrombin were seen. The abnormal prothrombin had a mobility more anodal than that of normal prothrombin, but less anodal than that of acarboxyprothrombin. The abnormal prothrombin, in contrast to acarboxyprothrombin, adsorbed readily to both aluminum hydroxide and barium citrate, and could be identified by two-dimensional immunoelectrophoresis of a barium citrate eluate. We suspect that the abnormal variant represents a partially carboxylated prothrombin.
一名18个月大的儿童，没有肝病、吸收不良或长期摄入香豆素化合物的证据，却被发现血浆中凝血因子II、VII、IX和X缺乏。通过免疫技术（抗体中和及免疫电泳）对凝血因子II和X进行检测，结果显示这些因子的抗原活性正常或升高，这表明患者血浆中存在异常蛋白质变体。在含钙的患者血浆二维免疫电泳中，观察到了正常和异常的凝血酶原群体。异常凝血酶原的迁移率比正常凝血酶原更偏向阳极，但比脱羧凝血酶原的阳极迁移率要小。与脱羧凝血酶原不同，异常凝血酶原很容易吸附到氢氧化铝和柠檬酸钡上，并且可以通过柠檬酸钡洗脱液的二维免疫电泳进行鉴定。我们怀疑这种异常变体代表一种部分羧化的凝血酶原。
