Purification of an active proteolytic fragment of the membrane attachment site for human erythrocyte spectrin.

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作者信息

Bennett V

出版信息

J Biol Chem. 1978 Apr 10;253(7):2292-9.

PMID:632270

Abstract

摘要

相似文献

Purification of an active proteolytic fragment of the membrane attachment site for human erythrocyte spectrin.

J Biol Chem. 1978 Apr 10;253(7):2292-9.

Identification by peptide analysis of the spectrin-binding protein in human erythrocytes.通过肽分析鉴定人红细胞中的血影蛋白结合蛋白。

J Biol Chem. 1979 Apr 10;254(7):2526-32.

Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin.

J Biol Chem. 1979 Apr 10;254(7):2533-41.

The effect of endogenous proteases on the spectrin binding proteins of human erythrocytes.内源性蛋白酶对人红细胞血影蛋白结合蛋白的作用。

Biochim Biophys Acta. 1980 Jun 6;598(3):517-27. doi: 10.1016/0005-2736(80)90032-2.

Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1.

Proc Natl Acad Sci U S A. 1979 Oct;76(10):5192-6. doi: 10.1073/pnas.76.10.5192.

State of spectrin phosphorylation does not affect erythrocyte shape or spectrin binding to erythrocyte membranes.血影蛋白的磷酸化状态不影响红细胞的形状或血影蛋白与红细胞膜的结合。

J Biol Chem. 1980 Feb 25;255(4):1259-65.

Rotational dynamics of spectrin in solution and ankyrin bound in human erythrocyte membrane.血影蛋白在溶液中的旋转动力学以及人红细胞膜中结合的锚蛋白。

FEBS Lett. 1980 May 5;113(2):231-4. doi: 10.1016/0014-5793(80)80598-9.

The molecular basis for membrane - cytoskeleton association in human erythrocytes.人类红细胞中膜 - 细胞骨架关联的分子基础。

J Cell Biochem. 1982;18(1):49-65. doi: 10.1002/jcb.1982.240180106.

Proteolytic fragmentation of spectrin:effect of removal of terminal phosphopeptides on spectrin binding to human erythrocyte membranes.血影蛋白的蛋白水解片段化：去除末端磷酸肽对血影蛋白与人红细胞膜结合的影响。

Prog Clin Biol Res. 1979;30:531-4.

Spectrin tetramer-dimer equilibrium and the stability of erythrocyte membrane skeletons.血影蛋白四聚体-二聚体平衡与红细胞膜骨架的稳定性

Nature. 1980 Jun 19;285(5766):586-8. doi: 10.1038/285586a0.

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