Solubilization of sarcoplasmic reticulum membranes by sodium dodecylsulphate. A Fourier-transform infrared spectroscopic study.
In order to improve our understanding of membrane protein solubilization by sodium dodecylsulphate, sarcoplasmic reticulum vesicles have been treated with this surfactant at different detergent: protein mole ratios. Effects on Ca2(+)-ATPase activity, membrane protein solubilization, and protein conformation have been independently monitored, and correlations among the various parameters have been observed. The thermal denaturation of sarcoplasmic reticulum proteins in the presence of sodium dodecylsulphate has also been characterized spectroscopically.
Prado
A
A
Department of Biochemistry, University of the Basque Country, Bilbao, Spain.
Muga
A
A
Castresana
J
J
Goñi
F M
FM
Arrondo
J L
JL
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002458:Cell Fractionation / Q000379:methods; D005583:Fourier Analysis; D009132:Muscles / Q000648:ultrastructure*; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000187:drug effects / Q000648:ultrastructure*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D012995:Solubility; D013055:Spectrophotometry, Infrared / Q000379:methods
D012967:Sodium Dodecyl Sulfate; D000252:Calcium-Transporting ATPases