Howe C L, Sacramone L M, Mooseker M S, Morrow J S
J Cell Biol. 1985 Oct;101(4):1379-85. doi: 10.1083/jcb.101.4.1379.
The spectrins isolated from chicken erythrocytes and chicken intestinal brush border, TW260/240, share a common alpha subunit and a tissue-specific beta subunit. The ability of these related proteins to bind human erythrocyte inside out vesicles (IOVs) and human erythrocyte ankyrin in vitro have been quantitatively compared with human erythrocyte spectrin. Chicken erythrocyte spectrin binds human IOVs and human ankyrin with affinities nearly identical to that for human erythrocyte spectrin. TW260/240 does not significantly bind to either IOVs or ankyrin. These results demonstrate a remarkable tissue preservation of ankyrin-binding capacity, even between diverse species, and confirm the role of the avian beta-spectrins in modulating this functionality. Avian brush border spectrin may represent a unique spectrin which serves primarily as a filament cross-linker and which does not interact strongly with membrane-associated proteins.
从鸡红细胞和鸡小肠刷状缘分离出的血影蛋白TW260/240，共享一个共同的α亚基和一个组织特异性的β亚基。已将这些相关蛋白在体外结合人红细胞内翻囊泡（IOV）和人红细胞锚蛋白的能力与人类红细胞血影蛋白进行了定量比较。鸡红细胞血影蛋白与人IOV和人锚蛋白的结合亲和力与人红细胞血影蛋白几乎相同。TW260/240与IOV或锚蛋白均无明显结合。这些结果表明，即使在不同物种之间，锚蛋白结合能力也能得到显著的组织保留，并证实了禽类β血影蛋白在调节这种功能中的作用。禽类刷状缘血影蛋白可能代表一种独特的血影蛋白，它主要作为细丝交联剂，与膜相关蛋白的相互作用不强。
