The Open Biochemistry Journal




ISSN: 1874-091X ― Volume 13, 2019

Properties of the SR Ca-ATPase in an Open Microsomal Membrane Preparation



A Fibich, C Jüngst, H.-J Apell*

Abstract

SR vesicles isolated from rabbit muscle were treated by a SDS incubation and subsequent dialysis to obtain open membrane fragments that allow a direct access to the luminal membrane surface and especially to the ion-binding sites in the P-E2 conformation of the Ca-ATPase. The open membrane fragments showed about 80% of the enzyme activity in the untreated membranes. Pump function was investigated by using electrochromic styryl dyes. The kinetic properties of cytoplasmic ion binding showed no significant differences between the Ca-ATPases in SR vesicles and in membrane fragments. From pH-dependent Ca2+ binding it could be deduced that due to the SDS treatment the density of negatively charged lipid was increased by one elementary charge per 12 lipid molecules. Major differences between Ca-ATPase from SR vesicles and membrane fragments were the respective fluorescence amplitudes. This effect is, however, produced by dye-lipid interaction and not by pump function. It was demonstrated that time-resolved kinetics may be study by the use of caged compounds such as caged ATP or caged calcium also in the case of the membrane fragments.

Keywords: Membrane fragments, ion binding, fluorescence, electrochromic dyes, pH effects.


Article Information


Identifiers and Pagination:

Year: 2008
Volume: 2
First Page: 91
Last Page: 99
Publisher Id: TOBIOCJ-2-91
DOI: 10.2174/1874091X00802010091

Article History:

Received Date: 23/4/2008
Revision Received Date: 16/5/2008
Acceptance Date: 26/5/2008
Electronic publication date: 9/6/2008
Collection year: 2008

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© Fibich et al.; Licensee Bentham Open.

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.5/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited.


* Address correspondence to these authors at the Department of Biology, University of Konstanz, 78464 Konstanz, Germany;E-mail: h-j.apell@uni-konstanz.de


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