Vizel E J, Tenenhouse H S, Scriver C R
Department of Biology, deBelle Laboratory for Biochemical Genetics, McGill University-Montreal Children's Hospital Research Institute, Quebec, Canada.
J Inherit Metab Dis. 1987;10(3):243-52. doi: 10.1007/BF01800070.
The X-linked dominant mutation, hypophosphataemia (gene symbol, Hyp) is expressed in the laboratory mouse as deficient phosphate transport at the renal brush border membrane (BBM) of proximal nephron. In an attempt to identify proteins which mediate phosphate transport, we treated renal BBM vesicles prepared from mutant male (Hyp/Y) and normal male (+/Y) littermates, with radiolabelled N-ethylmaleimide (NEM), in the presence or absence of arsenate of arsenate which is a competitive inhibitor of phosphate transport. Polyacrylamide gel electrophoresis revealed labelling of membrane proteins in the 40-45 kDa range; addition of arsenate during NEM treatment inhibited labelling. These findings indicate a 40-45 kDa protein as a component of the renal BBM phosphate transport system(s). We found no difference between protein labelling of the renal BBM from Hyp/Y and +/Y mice.
X连锁显性突变低磷血症(基因符号,Hyp)在实验小鼠中表现为近端肾单位肾刷状缘膜(BBM)处磷酸盐转运缺陷。为了鉴定介导磷酸盐转运的蛋白质,我们用放射性标记的N-乙基马来酰亚胺(NEM)处理从突变雄性(Hyp/Y)和正常雄性(+/Y)同窝小鼠制备的肾BBM囊泡,存在或不存在作为磷酸盐转运竞争性抑制剂的砷酸盐。聚丙烯酰胺凝胶电泳显示在40 - 45 kDa范围内的膜蛋白有标记;在NEM处理期间添加砷酸盐会抑制标记。这些发现表明一种40 - 45 kDa的蛋白质是肾BBM磷酸盐转运系统的一个组成部分。我们发现Hyp/Y和+/Y小鼠肾BBM的蛋白质标记没有差异。