期刊论文详细信息
FEBS Letters
Antibodies to the calmodulin‐binding Ca2+‐transport ATPase from smooth muscle
Wuytack, Frank1  Casteels, Rik1  Verbist, Jan1  Schutter, Greet De1 
[1] Laboratorium voor Fysiologie, Katholieke Universiteit Leuven, Campus Gasthuisberg, 3000 Leuven, Belgium
关键词: Calmodulin;    CaMg ATPase;    Erythrocyte;    Immunochemistry;    Sarcoplasmic reticulum;    Smooth muscle;    CaMg-ATPase;    (Ca2+ + Mg2+)-ATPase;    SDS;    Sodium-dodecylsulphate;    IgG;    immunoglobulin G;   
DOI  :  10.1016/0014-5793(83)80901-6
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Antibodies were raised against a calmodulin-binding CaMg-ATPase (Ca2+-transport ATPase) from smooth muscle. The binding of these antibodies to a number of related Ca2+-transport ATPases was studied. Antibodies to the calmodulin-binding ATPase from porcine antrum (stomach) smooth muscle do not only bind to this CaMg-ATPase, but also to the corresponding enzyme in porcine erythrocytes. However, they do not bind to the CaMg-ATPase from sarcoplasmic reticulum of porcine skeletal muscle. The binding of these antibodies to the CaMg-ATPase of smooth muscle, does not inhibit the enzyme activity.

【 授权许可】

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