Busch S
Institut für Pharmakologie, Universitätsklinikum Essen, Germany.
Biochim Biophys Acta. 1997 Apr 3;1325(1):13-6. doi: 10.1016/s0005-2736(97)00011-4.
We have cloned and sequenced the cDNA for a Na+/H+ exchanger (NHE) from Xenopus laevis oocytes. This cDNA contains an open reading frame encoding a protein of 782 amino acids with 12 putative transmembrane domains and a long cytoplasmic tail. The protein exhibits a strong homology at the amino acid level to the human NHE-1 as well as to the beta NHE from trout red blood cells: 69% and 58% respectively. Two potential N-linked glycosylation sites at Asn56 and Asn351 were identified. Three potential protein kinase C phosphorylation sites at the cytoplasmic tail were identified at Ser494, Thr726 and Ser747. RT-PCR revealed the expression of the X1-NHE in Xenopus heart, reticulocytes and skeletal muscle.
我们已经克隆并测序了非洲爪蟾卵母细胞中一种钠氢交换体（NHE）的cDNA。该cDNA包含一个开放阅读框，编码一个由782个氨基酸组成的蛋白质，具有12个假定的跨膜结构域和一条长的胞质尾巴。该蛋白质在氨基酸水平上与人类NHE-1以及鳟鱼红细胞中的β-NHE具有很强的同源性，分别为69%和58%。在Asn56和Asn351处鉴定出两个潜在的N-糖基化位点。在胞质尾巴的Ser494、Thr726和Ser747处鉴定出三个潜在的蛋白激酶C磷酸化位点。RT-PCR显示X1-NHE在非洲爪蟾的心脏、网织红细胞和骨骼肌中表达。
