SYNDEINS - SPECTRIN-BINDING PROTEIN(S) OF THE HUMAN-ERYTHROCYTE MEMBRANE

被引：150

作者：

YU, J ^{[1
]}

GOODMAN, SR ^{[1
]}

机构：

[1] HARVARD UNIV,BIOL LABS,CAMBRIDGE,MA 02138

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1979年 / 76卷 / 05期

关键词：

D O I：

10.1073/pnas.76.5.2340

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Two-dimensional tryptic and chymotryptic analyses of all the major bands in a sodium dodecyl sulfate/polyacrylamide gel of the human erythrocyte membrane show that each band has a characteristic map. However, band 2.1 (nomenclature of T.L. Steck) and several polypeptides below this band exhibit similar tryptic and chymotryptic peptide maps and thus appear to be a family of closely related proteins or degradation products. Furthermore, they all contain a subset of peptides that are accounted for by the peptides from two known spectrin-binding fragments. We show that both fragments derive from 2.1-related proteins and conclude that band 2.1 and its related proteins, which we name 'syndeins', bind spectrin and connect it to the erythrocyte membrane.

引用

页码：2340 / 2344

页数：5

共 22 条

[1]

BENNETT V, 1978, J BIOL CHEM, V253, P2292

[2]

BENNETT V, 1977, J BIOL CHEM, V252, P2753

[3] MECHANISM OF ATP-INDUCED SHAPE CHANGES IN HUMAN ERYTHROCYTE-MEMBRANES .2. ROLE OF ATP [J].