Structural properties of sarcoplasmic reticulum Ca 2+-ATPase as studied by intrinsic protein fluorescence

1. 1. From the intrinsic fluorescence spectral properties and fluorescence quenching experiments done with acrylamide and iodide, using native sarcoplasmic reticulum vesicles, purified ATPase and ATPase solubilized with 1% Triton X-100, it is deduced that practically all the fluorescent tryptophanyl...

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Published inInternational journal of biochemistry Vol. 19; no. 9; pp. 873 - 878
Main Authors Teruel, JoséA., Gómez-Fernández, Juan C.
Format Journal Article
LanguageEnglish
Published Elsevier B.V 1987
Subjects
Mops-3-( N-morpholino)propanesulfonic acid
DPPC-dipalmitoylphosphatidylcholine
DMPC-dimiristoylphosphatidylcholine
DPH-diphenylhexatriene
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Summary:1. 1. From the intrinsic fluorescence spectral properties and fluorescence quenching experiments done with acrylamide and iodide, using native sarcoplasmic reticulum vesicles, purified ATPase and ATPase solubilized with 1% Triton X-100, it is deduced that practically all the fluorescent tryptophanyl residues of this protein belong to a single population showing similar hydrophobic microenvironments. 2. 2. Both acrylamide and iodide seem to be able to penetrate through the sarcoplasmic reticulum membrane. 3. 3. The intrinsic fluorescence of the Ca 2+-ATPase due to tryptophan residues probably buried inside the membrane is used as a tool to follow thermotropic changes in membrane fluidity of reconstituted systems.
ISSN:0020-711X
DOI:10.1016/0020-711X(87)90248-5