Identification by peptide analysis of the spectrin-binding protein in human erythrocytes.
Identification by peptide analysis of the spectrin-binding protein in human erythrocytes.
复制标题
通过肽分析鉴定人红细胞中的血影蛋白结合蛋白。
DOI：
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发表时间：
1979
影响因子：
4.8
通讯作者：
D. Branton
中科院分区：
文献类型：
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作者：
E. Luna;G. Kidd;D. Branton
一维和二维肽图技术被用来鉴定产生72,000道尔顿α-胰凝乳酶片段的蛋白质，该片段先前被证明是血影蛋白的膜结合部位。72,000个道尔顿片段的多肽图谱与区带1、2、2.9、3、3.1、4.1和4.2的图谱非常不同，而与明显同源的多肽的图谱2.1、2.2、2.3和2.6非常相似。红细胞膜的有限蛋白分解可产生带3‘，这是另一种与血影蛋白结合活性有关的多肽。Band 3‘的多肽图谱与Band 2.1的图谱非常相似，表明Band 3’也是Band 2.1的蛋白水解区。结果表明，Band2.1和其他部分或全部相关多肽可能是人红细胞的血影蛋白结合蛋白(S)。
One-dimensional and two-dimensional peptide-mapping techniques are used to identify the protein which gives rise to the 72,000 dalton alpha-chymotryptic fragment previously shown to be the membrane attachment site for spectrin. Peptide maps of the 72,000 dalton fragment are very different from maps of Bands 1, 2, 2.9, 3, 3.1, 4.1, and 4.2 and very similar to maps of the apparently closely homologous polypeptides, Bands 2.1, 2.2, 2.3, and 2.6. Limited proteolysis of erythrocyte membranes is shown to generate Band 3', another polypeptide which has been associated with spectrin-binding activity. Peptide maps of Band 3' are very similar to maps of Band 2.1, suggesting that Band 3' is also a proteolytic fragment of Band 2.1. It is concluded that Band 2.1 and possibly some or all of the other, related polypeptides which electrophorese in the 2 region is (are) the spectrin-binding protein(s) of the human erythrocyte.