Intramolecular cross-linking at the active site of the Ca2+-ATPase of sarcoplasmic reticulum. High and low affinity nucleotide binding and evidence of active site closure in E2-P.-Reference-Cited by-同舟云学术

Intramolecular cross-linking at the active site of the Ca2+-ATPase of sarcoplasmic reticulum. High and low affinity nucleotide binding and evidence of active site closure in E2-P.

Published:1987-09 Issue:27 Volume:262 Page:12977-12983
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ross D C,McIntosh D B

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference63 articles.

1. Amino-acid sequence of a Ca2+ + Mg2+ -dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence

2. Energy Interconversion by the Ca2+-Dependent ATPase of the Sarcoplasmic Reticulum

3. Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ions

4. Occurrence and Characteristics of a Rapid Exchange of Phosphate Oxygens Catalyzed by Sarcoplasmic Reticulum Vesicles

5. Phosphorylation of the calcium adenosine triphosphatase of sarcoplasmic reticulum: rate-limiting conformational change followed by rapid phosphoryl transfer

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