Site-directed Disulfide Mapping of Helices M4 and M6 in the Ca2+ Binding Domain of SERCA1a, the Ca2+ ATPase of Fast Twitch Skeletal Muscle Sarcoplasmic Reticulum-Reference-Cited by-同舟云学术

Site-directed Disulfide Mapping of Helices M4 and M6 in the Ca2+ Binding Domain of SERCA1a, the Ca2+ ATPase of Fast Twitch Skeletal Muscle Sarcoplasmic Reticulum

Published:1997-12 Issue:50 Volume:272 Page:31412-31419
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Rice William J.,Green N. Michael,MacLennan David H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference52 articles.

1. Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the Ca2+ transport activity of the Ca2+-ATPase expressed in COS-1 cells.

2. Location of high affinity Ca2 +-binding sites within the predicted transmembrahe domain of the sarco-plasmic reticulum Ca2+-ATPase

3. Functional consequences of alterations to polar amino acids located in the transmembrane domain of the Ca2(+)-ATPase of sarcoplasmic reticulum.

4. Sequential mechanism of calcium binding and translocation in sarcoplasmic reticulum adenosine triphosphatase.

5. Lumenal Ca2+ Dissociation from the Phosphorylated Ca2+-ATPase of the Sarcoplasmic Reticulum Is Sequential

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