Ohno S, Payne H W, Morrison M, Beutler E
Science. 1966 Aug 26;153(3739):1015-6. doi: 10.1126/science.153.3739.1015.
Starch-gel electrophoresis of extracts of human liver revealed the presence of a new hexose-6-phosphate dehydrogenase that was slower-moving at pH 8.6 than the sex-linked glucose-6-phosphate dehydrogenase. When the gel plate was stained, galactose-6-phos phate being used as a substrate, this enzyme band stained intensely, but the sex-linked glucose-6-phosphate dehydro genase failed to stain. This new human enzyme may well be homologous with the autosomally inherited glucose-6-phosphate dehydrogenase of the deer mouse (Peromyscus maniculatus), re ported by Shaw and Barto.
人肝提取物的淀粉凝胶电泳显示存在一种新的6-磷酸己糖脱氢酶,在pH 8.6条件下,其迁移速度比性连锁的6-磷酸葡萄糖脱氢酶慢。当用6-磷酸半乳糖作为底物对凝胶板进行染色时,该酶带染色很深,但性连锁的6-磷酸葡萄糖脱氢酶未染色。这种新的人类酶很可能与肖和巴托报道的鹿鼠(白足鼠)常染色体遗传的6-磷酸葡萄糖脱氢酶同源。