King A, Melton D W
Department of Molecular Biology, Edinburgh University, UK.
Nucleic Acids Res. 1987 Dec 23;15(24):10469-81. doi: 10.1093/nar/15.24.10469.
The isolation of cDNA clones for hypoxanthine-guanine phosphoribosyltransferase (HPRT) from the human malarial parasite, Plasmodium falciparum, is described. Northern analysis indicates that P. falciparum HPRT mRNA is the same size as that coding for mammalian HPRT. The predicted amino acid sequence of the P. falciparum HPRT protein shows extensive homology to the mammalian enzyme. Homology between the two proteins occurs in distinct blocks and a putative catalytic binding domain in the centre of the protein is also conserved. Five out of the seven characterised mammalian HPRT missense mutations map to regions which are conserved in the P. falciparum protein.
本文描述了从人类疟原虫恶性疟原虫中分离次黄嘌呤 - 鸟嘌呤磷酸核糖转移酶(HPRT)cDNA克隆的过程。Northern分析表明,恶性疟原虫HPRT mRNA的大小与编码哺乳动物HPRT的mRNA相同。恶性疟原虫HPRT蛋白的预测氨基酸序列与哺乳动物酶显示出广泛的同源性。两种蛋白质之间的同源性出现在不同的区域,并且蛋白质中心的一个假定催化结合域也保守。七个已鉴定的哺乳动物HPRT错义突变中有五个映射到恶性疟原虫蛋白质中保守的区域。