Spectrin and ankyrin in brain.
Spectrin and ankyrin in brain.
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脑中的血影蛋白和锚蛋白。
DOI：
10.1002/cm.970030527
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Davis,J
中科院分区：
文献类型：
--
作者：
Bennett,V;Davis,J
哺乳动物红细胞血影蛋白和猪脑血影蛋白之间的进一步相似性已通过（a）与脑α链和红细胞β链形成杂合分子和（B）在脑膜中鉴定锚蛋白得到证实。由脑α链和红细胞β链制备的混合血影蛋白分子通过低角度旋转阴影显示为双链杆（二聚体）与红细胞β亚基杂交的125 I标记的脑α链获得了与红细胞膜上锚蛋白位点结合的能力。将这些多肽转移到硝酸纤维素后，125 I标记的脑α链仅与红细胞和脑血影蛋白的β亚基结合十二烷基硫酸钠（SDS）凝胶纸。因此，脑血影蛋白和哺乳动物红细胞血影蛋白具有共同的功能位点，参与其亚基的关联。脑和红细胞膜相似性的其他证据是在脑中发现了一种210，000 Mr的膜蛋白，该蛋白与红细胞锚蛋白交叉反应，并具有72，000 Mr的水溶性结构域，该结构域由蛋白酶消化产生。脑锚蛋白的72，000 Mr结构域已通过红细胞血影蛋白-琼脂糖凝胶亲和层析分离，并被证明直接结合红细胞和脑血影蛋白。脑72，000 Mrfragment与红细胞72，000 Mrankyrin片段具有不同的肽图谱，因此不是红细胞污染的结果。
Further similarity between mammalian erythrocyte spectrin and pig brain spectrin has been demonstrated by (a) formation of hybrid molecules with brain α‐chains and erythrocyte β‐chains and by (b) identification of an ankyrin protein in brain membranes. Hybrid spectrin molecules prepared from brain α‐chains and erythrocyte β‐chains were visualized by low‐angle rotary shadowing as double‐stranded rods (dimers) 100 nM in length.125I‐labeled brain α‐chain that was hybridized with erythrocyte β‐subunit acquired ability to bind to ankyrin sites on erythrocyte membranes.125I‐labeled brain α‐chain bound only to β‐subunits of erythrocyte and brain spectrin following transfer of these polypeptides to nitrocellulose paper from sodium dodecyl sulfate (SDS) gels. Thus brain spectrin and mammalian erythrocyte spectrin have shared functional sites involved in association of their subunits. Additional evidence for similarity of brain and erythrocyte membranes is the finding of a 210,000Mrmembrane protein in brain that cross‐reacts with erythrocyte ankyrin and has a water‐soluble domain of 72,000Mrthat is produced by protease digestion. The 72,000Mrdomain of brain ankyrin has been isolated by affinity chromatography on erythrocyte spectrin‐Sepharose, and was demonstrated to bind directly to erythrocyte and brain spectrin. The brain 72,000Mrfragment has distinct peptide maps from the erythrocyte 72,000Mrankyrin fragment and thus is not a result of erythrocyte contamination.