Ma Y, Zimmer W E, Riederer B M, Bloom M L, Barker J E, Goodman S M, Goodman S R
Department of Structural and Cellular Biology, University of South Alabama, School of Medicine, Mobile 36688.
Brain Res Mol Brain Res. 1993 Apr;18(1-2):87-99. doi: 10.1016/0169-328x(93)90176-p.
The amino acid sequence of mouse brain beta spectrin (beta fodrin), deduced from the nucleotide sequence of complementary DNA clones, reveals that this non-erythroid beta spectrin comprises 2363 residues, with a molecular weight of 274,449 Da. Brain beta spectrin contains three structural domains and we suggest the position of several functional domains including f-actin, synapsin I, ankyrin and spectrin self association sites. Analysis of deduced amino acid sequences indicated striking homology and similar structural characteristics of brain beta spectrin repeats beta 11 and beta 12 to globins. In vitro analysis has demonstrated that heme is capable of specific attachment to brain spectrin, suggesting possible new functions in electron transfer, oxygen binding, nitric oxide binding or heme scavenging.
从小鼠脑β-血影蛋白（β- fodrin）互补DNA克隆的核苷酸序列推导而来的氨基酸序列显示，这种非红细胞β-血影蛋白由2363个残基组成，分子量为274,449道尔顿。脑β-血影蛋白包含三个结构域，我们推测了几个功能域的位置，包括f-肌动蛋白、突触素I、锚蛋白和血影蛋白自身结合位点。对推导的氨基酸序列的分析表明，脑β-血影蛋白的β11和β12重复序列与球蛋白具有显著的同源性和相似的结构特征。体外分析表明，血红素能够特异性地附着于脑血影蛋白，提示其在电子传递、氧结合、一氧化氮结合或血红素清除方面可能具有新功能。
