Hempelmann E, Schirmer R H, Fritsch G, Hundt E, Gröschel-Stewart U
Mol Biochem Parasitol. 1987 Feb;23(1):19-24. doi: 10.1016/0166-6851(87)90182-4.
An improved protein-blotting procedure and a thin layer isoelectric focusing technique are introduced to study glutathione reductase and methemoglobin (Met-Hb). According to our results, there is only one form of glutathione reductase in normal red blood cells. A similar protein was shown to be present at higher concentration in isolated merozoites. Both proteins have a subunit Mr of ca. 50,000 and react with anti-human glutathione reductase serum. Red cells with schizonts do not possess a higher proportion of Met-Hb than non-parasitized erythrocytes. This finding suggests that Met-Hb is not an indicator of metabolic alterations in malaria-infected erythrocytes.
引入了一种改进的蛋白质印迹程序和一种薄层等电聚焦技术来研究谷胱甘肽还原酶和高铁血红蛋白(Met-Hb)。根据我们的结果,正常红细胞中只有一种形式的谷胱甘肽还原酶。在分离的裂殖子中发现一种类似的蛋白质浓度更高。两种蛋白质的亚基分子量约为50,000,并与抗人谷胱甘肽还原酶血清发生反应。含有裂殖体的红细胞中Met-Hb的比例并不比未感染疟原虫的红细胞高。这一发现表明,Met-Hb不是疟疾感染红细胞代谢改变的指标。