Drickamer L K
J Biol Chem. 1978 Oct 25;253(20):7242-8.
The NH2-terminal sequence and carbohydrate attachment site of the 95,000-dalton transmembrane polypeptide (Band 3) from human erythrocyte membranes have been studied. The blocked NH2-terminal sequence is Ac-Met-Glu-Glu; the presence of this sequence in specific fragments of the polypeptide confirms that the end of the polypeptide which is inside the cell is the NH2-terminal. The carbohydrate associated with the Band 3 polypeptide appears to be attached at a single site in the COOH-terminal third of the molecule, to a region with composition Asx1Ser2; this confirms that part of the polypeptide toward the COOH-terminal is outside the cell. The carbohydrate structure appears to be extremely heterogeneous both in size and composition, which probably causes the Band 3 polypeptide to migrate as a diffuse band on dodecyl sulfate gel electrophoresis.
对人红细胞膜上95,000道尔顿跨膜多肽（带3）的氨基末端序列和碳水化合物连接位点进行了研究。封闭的氨基末端序列是Ac-Met-Glu-Glu；该序列在多肽特定片段中的存在证实了位于细胞内的多肽末端是氨基末端。与带3多肽相关的碳水化合物似乎连接在分子羧基末端三分之一处的单个位点上，连接到一个组成为Asx1Ser2的区域；这证实了多肽朝向羧基末端的部分位于细胞外。碳水化合物结构在大小和组成上似乎极其不均一，这可能导致带3多肽在十二烷基硫酸钠凝胶电泳上以弥散条带形式迁移。
