Literature DB >> 2936395

Occlusion of Ca2+ in soluble monomeric sarcoplasmic reticulum Ca2+-ATPase.

B Vilsen, J P Andersen.   

Abstract

Sarcoplasmic reticulum Ca2+-ATPase solubilized in monomeric form by nonionic detergent was reacted with CrATP in the presence of 45Ca2+. A Ca2+-occluded complex formed, which was stable during high performance liquid chromatography in the presence of excess non-radioactive Ca2+. The elution position corresponded to monomeric Ca2+-ATPase. It is concluded that a single Ca2+-ATPase polypeptide chain provides the full structural basis for Ca2+ occlusion.

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Year:  1986        PMID： 2936395     DOI： 10.1016/0005-2736(86)90089-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  5 in total

1.  Crosslinking the active site of sarcoplasmic reticulum Ca(2+)-ATPase completely blocks Ca2+ release to the vesicle lumen.

Authors:  D B McIntosh; D C Ross; P Champeil; F Guillain
Journal:  Proc Natl Acad Sci U S A       Date:  1991-08-01       Impact factor: 11.205

Review 2.  Structural basis for E1-E2 conformational transitions in Na,K-pump and Ca-pump proteins.

Authors:  P L Jørgensen; J P Andersen
Journal:  J Membr Biol       Date:  1988-07       Impact factor: 1.843

3.  Electron microscopic analysis of two-dimensional crystals of the Ca2+-transport ATPase--a freeze-fracture study.

Authors:  H P Ting-Beall; F M Burgess; L Dux; A Martonosi
Journal:  J Muscle Res Cell Motil       Date:  1987-06       Impact factor: 2.698

4.  Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p.

Authors:  Guillaume Lenoir; Patrick Williamson; Catheleyne F Puts; Joost C M Holthuis
Journal:  J Biol Chem       Date:  2009-05-02       Impact factor: 5.157

5.  Localization of E1-E2 conformational transitions of sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling.

Authors:  J P Andersen; B Vilsen; J H Collins; P L Jørgensen
Journal:  J Membr Biol       Date:  1986       Impact factor: 1.843
  5 in total

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