Unsaturated aminophospholipids are preferentially retained by the fast skeletal muscle CaATPase during detergent solubilization
- 1 May 1991
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 286 (2) , 346-352
- https://doi.org/10.1016/0003-9861(91)90050-s
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Phospholipid fatty acyl chain asymmetry in the membrane bilayer of isolated skeletal muscle sarcoplasmic reticulumBiochemistry, 1987
- Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequencesCell, 1986
- The separate profile structures of the functional calcium pump protein and the phospholipid bilayer within isolated sarcoplasmic reticulum membranes determined by X-ray and neutron diffractionBiochimica et Biophysica Acta (BBA) - Biomembranes, 1985
- Phase behavior of membranes reconstituted from dipentadecanoylphosphatidylcholine and the magnesium-dependent, calcium-stimulated adenosine triphosphatase of sarcoplasmic reticulum: evidence for a disrupted lipid domain surrounding proteinBiochemistry, 1985
- Fluidity of sarcoplasmic reticulum membranes investigated with dipyrenylpropane, an intramolecular excimer probeBiochemistry, 1982
- A new high-yield procedure for the purification of the non-specific phospholipid transfer protein from rat liverBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1981
- Neuronal membrane lipid asymmetryLife Sciences, 1979
- Retention of enzyme activity by detergent-solubilized sarcoplasmic Ca2+ion-activated ATPaseBiochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970