Phase transitions of Acholeplasma laidlawii membranes. The involvement of Mg(2+)-ATPase in the C transition.
Highly sensitive differential scanning calorimetry has been employed to study the phase transitions of A. laidlawii membrane. The DSC curves obtained show five distinct transitions between 20 and 80 degrees C which contain a reversible lipid thermotropic transition at about 37 degrees C and four irreversible denaturation transitions of the membrane proteins occurred at about 44 degrees C, 52 degrees C, 62 degrees C, and 67 degrees C, respectively. Total enthalpy of the thermal denaturation of membrane proteins is 3.4 +/- 0.5 cal/g. Further study of A. laidlawii membrane preparations by means of thermal gel analysis and enzyme activity measurements at various temperatures provided information that the third peak (C transition) of the DSC curve involved primarily with Mg(2+)-ATPase on A. laidlawii membranes.
Chen
J W
JW
Institute of Biophysics, Academia Sinica, Beijing, China.
Hu
L Y
LY
Hwang
F
F
D000128:Acholeplasma laidlawii / Q000737:chemistry* / Q000201:enzymology / Q000648:ultrastructure; D017301:Ca(2+) Mg(2+)-ATPase / Q000737:chemistry / Q000378:metabolism*; D002152:Calorimetry, Differential Scanning; D002462:Cell Membrane / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000737:chemistry; D011489:Protein Denaturation; D013816:Thermodynamics
D008565:Membrane Proteins; D017301:Ca(2+) Mg(2+)-ATPase