Wilson J M, Daddona P E, Otoadese T, Kelley W N
J Lab Clin Med. 1982 Feb;99(2):163-74.
Elevated levels of APRT activity are found in erythrocytes from most patients with a primary deficiency of HPRT. A twofold elevation of APRT activity has also been measured in hemolysate from one patient with a deficiency of both OPRT and ODC activity. In an attempt to further define the mechanisms responsible for these apparent alterations in APRT expression, we have studied the catalytic, immunochemical, and electrophoretic properties of APRT in erythrocytes from patients with these inborn errors of purine and pyrimidine metabolism. We have found that the elevated activity of APRT in HPRT-deficient erythrocytes results from an increased amount of a catalytically normal APRT protein. Immunochemical and electrophoretic studies that this APRT protein is structurally normal. One patient with a deficiency of OPRT-ODC demonstrated a fourfold increase in APRT protein; this enzyme was catalytically less efficient than APRT from normal controls.
在大多数原发性次黄嘌呤-鸟嘌呤磷酸核糖转移酶（HPRT）缺乏的患者红细胞中，发现腺嘌呤磷酸核糖转移酶（APRT）活性升高。在一名同时缺乏乳清酸磷酸核糖转移酶（OPRT）和鸟氨酸脱羧酶（ODC）活性的患者的溶血产物中，也检测到APRT活性升高了两倍。为了进一步确定导致APRT表达出现这些明显变化的机制，我们研究了患有这些嘌呤和嘧啶代谢先天性缺陷的患者红细胞中APRT的催化、免疫化学和电泳特性。我们发现，HPRT缺乏的红细胞中APRT活性升高是由于催化正常的APRT蛋白量增加所致。免疫化学和电泳研究表明，这种APRT蛋白在结构上是正常的。一名OPRT-ODC缺乏的患者显示APRT蛋白增加了四倍；这种酶的催化效率低于正常对照的APRT。
