Schröter W, Tillmann W
Klin Wochenschr. 1977 Apr 15;55(8):393-6. doi: 10.1007/BF01488625.
The deficient red cell enzyme glucosephosphate isomerase (GPI) was characterized in a patient of German origin who had already been described, with congenital nonspherocytic hemolytic anemia, and in his heterozygous parents. The variant enzyme differs from the known GPI variant enzyme differs from the known GPI variants by the electrophoretic mobility, the thermal stability, and the leukocyte activity. No differences are found between normal GPI and the variant regarding the affinity to fructose-6-phosphate, the pH optimum and the thermal optimum. Since the electrophoretic pattern and the properties of the parenteral GPI are identical the propositus seems to be homozygous for an abnormal allele and not double-heterozygous as some other cases with GPI deficiency are. Recently, immunological studies have shown that the variant differs from other similar variants. According to the birthplace of the patient the variant is called "Paderborn".
在一名患有先天性非球形细胞溶血性贫血的德裔患者及其杂合子父母身上，对缺乏的红细胞酶葡萄糖磷酸异构酶（GPI）进行了特征分析。该变异酶在电泳迁移率、热稳定性和白细胞活性方面与已知的GPI变异体不同。在对果糖-6-磷酸的亲和力、最适pH值和最适温度方面，正常GPI与变异体之间未发现差异。由于亲本GPI的电泳图谱和特性相同，先证者似乎对异常等位基因是纯合的，而不像其他一些GPI缺乏症病例那样是双杂合的。最近，免疫学研究表明该变异体与其他类似变异体不同。根据患者的出生地，该变异体被称为“帕德博恩”。
