LIMITED PROTEOLYSIS OF HUMAN-ERYTHROCYTE CA-2+-ATPASE IN MEMBRANE-BOUND FORM - IDENTIFICATION OF CALMODULIN-BINDING FRAGMENTS

被引：14

作者：

EMELYANENKO, EI

SHAKHPARONOV, MI

MODYANOV, NN

机构：

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1985年 / 126卷 / 01期

关键词：

D O I：

10.1016/0006-291X(85)90593-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

引用

页码：214 / 219

页数：6

共 50 条

[1] ISOLATION AND CHARACTERIZATION OF THE CALMODULIN-BINDING REGION OF HUMAN-ERYTHROCYTE PLASMA-MEMBRANE CA-2+-ATPASE
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[2] INTERACTION OF CALMODULIN AND ITS FRAGMENTS WITH ERYTHROCYTE-MEMBRANE CA-2+-ATPASE
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[4] IDENTIFICATION OF THE CALMODULIN-BINDING DOMAIN OF HUMAN-ERYTHROCYTE SPECTRIN
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[6] EFFECTS OF FATTY-ACIDS ON ACTIVITY AND CALMODULIN BINDING OF CA-2+-ATPASE OF HUMAN-ERYTHROCYTE MEMBRANES
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[7] TARGET SIZES OF HUMAN-ERYTHROCYTE MEMBRANE CA-2+-ATPASE AND MG-2+-ATPASE ACTIVITIES IN THE PRESENCE AND ABSENCE OF CALMODULIN
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[8] FURTHER CHARACTERIZATION OF CALPAIN-MEDIATED PROTEOLYSIS OF THE HUMAN-ERYTHROCYTE PLASMA-MEMBRANE CA-2+-ATPASE
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[9] STIMULATION OF THE PURIFIED ERYTHROCYTE CA-2+-ATPASE BY TRYPTIC FRAGMENTS OF CALMODULIN
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[10] CONTROLLED PROTEOLYSIS OF THE PURIFIED CA-2+-ATPASE OF THE ERYTHROCYTE-MEMBRANE
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