Calorimetric investigation of the NABH4-modified bacteriorhodopsin in purple membrane from Halobacterium halobium.
Comparative differential scanning calorimetric study of intact purple membranes from Halobacterium halobium and when 50% of bacteriorhodopsin molecules were cut off by NaBH4 in the dark shows that two peaks beneath the overall endotherms correspond to a process of bacteriorhodopsin denaturation. These results suggest a different structural organization of two populations of bacteriorhodopsin in intact dark-adapted purple membranes.
Shnyrov
V L
VL
Departamento de Bioquímica y Biología Molecular, Facultad de Biología, Universidad de Salamanca, Spain.
D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism; D001894:Borohydrides / Q000494:pharmacology*; D002152:Calorimetry, Differential Scanning / Q000379:methods; D003624:Darkness; D019617:Halobacterium salinarum / Q000378:metabolism*; D006358:Hot Temperature; D011489:Protein Denaturation
D001894:Borohydrides; D001436:Bacteriorhodopsins; C025364:sodium borohydride