Wilson J M, Kobayashi R, Fox I H, Kelley W N
J Biol Chem. 1983 May 25;258(10):6458-60.
A mutant form of human hypoxanthine-guanine phosphoribosyltransferase (HPRTToronto) was isolated from erythrocytes of a male patient with gout due to a partial deficiency of enzyme activity. The tryptic peptides of HPRTToronto were mapped by reverse-phase high pressure liquid chromatography in an attempt to define the precise abnormality in its primary structure. Sequence analysis of the single aberrant peptide in HPRTToronto revealed an arginine to glycine amino acid substitution at position 50. A single nucleotide change in the codon for arginine 50 (CGA leads to GGA) could explain this substitution.
从一名因酶活性部分缺乏而患痛风的男性患者的红细胞中分离出一种人类次黄嘌呤 - 鸟嘌呤磷酸核糖转移酶的突变形式（HPRT多伦多型）。通过反相高压液相色谱法对HPRT多伦多型的胰蛋白酶肽段进行图谱分析，试图确定其一级结构中的精确异常。对HPRT多伦多型中单个异常肽段的序列分析显示，第50位氨基酸发生了从精氨酸到甘氨酸的替换。精氨酸50密码子（CGA变为GGA）中的单个核苷酸变化可以解释这种替换。
