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- W2289222136 abstract "Publisher Summary This chapter discusses the tryptophan (Trp) reactivity. Trp side chains of proteins react readily with N -bromo-succinimide (NBS) under mild conditions to give the oxindole derivative, with loss of the characteristic 280-nm indole absorbance. NBS from commercial sources is usually pale yellow because of the presence of free bromine, which can interfere with spectroscopic studies and may promote unwanted side reactions. Satisfactory purification can be obtained by recrystallization. Components in the system other than Trp react well with NBS under few conditions, in particular the tyrosine, histidine, and—SH groups of the protein and lipids from the solubilized disk membranes. Reaction of free retinal with NBS has also been reported. Both rhodopsin and bacteriorhodopsin require unusually high molar ratios of NBS for complete reaction. The NBS reaction can be carried out with intact membrane suspensions by omitting detergent from the mixture, but the extent of Trp oxidation can be difficult to follow directly because of light scattering." @default.
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- W2289222136 date "1982-01-01" @default.
- W2289222136 modified "2023-10-16" @default.
- W2289222136 title "[41] Tryptophan reactivity" @default.
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- W2289222136 doi "https://doi.org/10.1016/s0076-6879(82)81043-4" @default.
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