A Remarkably Stable Phosphorylated Form of Ca2+-ATPase Prepared from Ca2+-loaded and Fluorescein Isothiocyanate-labeled Sarcoplasmic Reticulum Vesicles-Reference-Cited by-同舟云学术

A Remarkably Stable Phosphorylated Form of Ca2+-ATPase Prepared from Ca2+-loaded and Fluorescein Isothiocyanate-labeled Sarcoplasmic Reticulum Vesicles

Published:2001-02 Issue:8 Volume:276 Page:5795-5803
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Champeil Philippe,Henao Fernando,Lacapère Jean-Jacques,McIntosh David B.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference57 articles.

1. Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labelled selectively with fluorescein

2. Identification of a labelled peptide after stoicheiometric reaction of fluorescein isothiocyanate with the Ca2+ -dependent adenosine triphosphatase of sarcoplasmic reticulum

3. Dynamic interconversions of phosphorylated and n0n-phosphorylated intermediates of the Ca-ATPase from sarcoplasmic reticulum followed in a flourescein-labeled enzyme

4. Interaction of magnesium and inorganic phosphate with calcium-deprived sarcoplasmic reticulum adenosine triphosphatase as reflected by organic solvent induced perturbation

5. ATP regulation of sarcoplasmic reticulum Ca2+-ATPase. Metal-free ATP and 8-bromo-ATP bind with high affinity to the catalytic site of phosphorylated ATPase and accelerate dephosphorylation.

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