Unexpected Phosphoryl Transfer from Asp351 to Fluorescein Attached to Lys515 in Sarcoplasmic Reticulum Ca2+-ATPase-Reference-Cited by-同舟云学术

Unexpected Phosphoryl Transfer from Asp351 to Fluorescein Attached to Lys515 in Sarcoplasmic Reticulum Ca2+-ATPase

Published:2008-05-24 Issue:24 Volume:47 Page:6386-6393
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

McIntosh David B.¹,Montigny Cédric¹,Champeil Philippe¹

Affiliation:

1. Institute of Infectious Diseases and Molecular Medicine, Division of Chemical Pathology, and National Health Laboratory Services, University of Cape Town, South Africa, CNRS, URA 2096 (Protéines Membranaires Transductrices d'Énergie), F-91191 Gif-sur-Yvette, France, and CEA, iBiTec-S (Institut de Biologie et Technologies de Saclay), F-91191 Gif-sur-Yvette, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800290q

Reference21 articles.

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

2. Interaction of Fluorescein Isothiocyanate with Nucleotide-Binding Sites of the Ca-ATPase from Sarcoplasmic Reticulum

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

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

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

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