Light-induced reaction of dicyclohexylcarbodiimide with bacteriorhodopsin

Bacteriorhodopsin solubilized in Triton X-100 micelles undergoes a light-induced reaction with [ 14C]-dicyclohexylcarbodiimide at pH 7.5. The reaction has three consequences: 1) incorporation of radioactivity into bacteriorhodopsin, 2) irreversible bleaching of the retinal chromophore, and 3) altera...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 101; no. 2; pp. 653 - 657
Main Authors Renthal, R., Dawson, N., Villarreal, L.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 30.07.1981
Subjects
bacteriorhodopsin
Bacteriorhodopsins
Carbodiimides
Carotenoids
Detergents
Dicyclohexylcarbodiimide
Halobacterium
Halobacterium halobium
Kinetics
Light
Micelles
Octoxynol
Polyethylene Glycols
Protein Binding
purple membranes
solubilization
Triton X-100
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Summary:Bacteriorhodopsin solubilized in Triton X-100 micelles undergoes a light-induced reaction with [ 14C]-dicyclohexylcarbodiimide at pH 7.5. The reaction has three consequences: 1) incorporation of radioactivity into bacteriorhodopsin, 2) irreversible bleaching of the retinal chromophore, and 3) alteration of the CNBr cleavage pattern. Reverse phase chromatography of the CNBr fragments from the modified bacteriorhodopsin reveals two new peptide fractions. The major fraction (91%) consists of two peptides of apparent molecular weights 10,700 and 5,400. N-terminal analysis suggests these peptides are bacteriorhodopsin residues 119–209 and 69–118, respectively. The modifications of these peptides are at sites that are exposed or activated by light, a property expected of groups involved in moving H + across the purple membrane during proton pumping.
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(81)91308-5