Murayama J I, Tomita M, Hamada A
J Membr Biol. 1982;64(3):205-15. doi: 10.1007/BF01870887.
The complete amino acid sequence of the major sialoglycoproteins of horse erythrocyte membranes, glycophorin HA, was determined by manual sequencing methods, using tryptic, chymotryptic, and cyanogen bromide fragments. Glycophorin HA is a polypeptide chain of 120 amino acid residues and contains 10 oligosaccharide units attached to the amino-terminal side of the molecule. Its amino terminus is pyroglutamic acid. All of the oligosaccharides are linked O-glycosidically to threonine or serine residues. The amino acid sequence is consistent with the transmembrane orientation of glycophorins. There is no significant homology between the glycosylated domains of horse, human, and porcine glycophorins, but there is a considerable homology between the hydrophobic domains of the three glycophorins, which interact with the lipid bilayer of the erythrocyte membrane.
采用胰蛋白酶、胰凝乳蛋白酶和溴化氰片段，通过手工测序方法测定了马红细胞膜主要唾液酸糖蛋白血型糖蛋白HA的完整氨基酸序列。血型糖蛋白HA是一条由120个氨基酸残基组成的多肽链，在分子的氨基末端侧含有10个寡糖单元。其氨基末端是焦谷氨酸。所有寡糖都通过O-糖苷键与苏氨酸或丝氨酸残基相连。该氨基酸序列与血型糖蛋白的跨膜方向一致。马、人和猪血型糖蛋白的糖基化结构域之间没有显著的同源性，但三种血型糖蛋白的疏水结构域之间存在相当程度的同源性，这些疏水结构域与红细胞膜的脂质双层相互作用。
