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Effect of ganglioside GM3 on the activity and conformation of reconstituted Ca 2+ ‐ATPase
Author(s) -
Wang L.H.,
Tu Y.P.,
Yang X.Y.,
Tsui Z.C.,
Yang F.Y.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00534-0
Subject(s) - endoplasmic reticulum , chemistry , atpase , circular dichroism , atp hydrolysis , ganglioside , skeletal muscle , biochemistry , biophysics , calcium atpase , enzyme , biology , anatomy
Trace amounts of gangliosides were found in rabbit skeletal muscle sarcoplasmic reticulum and their main part was shown, by high performance thin layer chromatography, to be GM3. Addition of GM3 to the soybean phospholipids used for reconstitution of proteoliposomes markedly increased ATP hydrolysis as well as Ca 2+ uptake activity of sarcoplasmic reticulum Ca 2+ ‐ATPase incorporated into the proteoliposomes. Conformation changes of Ca 2+ ‐ATPase induced by GM3 were also observed by intrinsic fluorescence and circular dichroism measurements.