Abstract
ABSTRACTThe interaction between tryptophan and α‐ketoglutaric acid (α‐KGA) was utilized for the quantitative estimation of tryptophan. Previous work enabled two sets of reaction conditions to be chosen which produced stable quantities of chromophore with wavelength of maximum absorbance (lDmax) at 358 nm. Both conditions produced Beer's Law plots over the concentration range 0‐l.8 mM tryptophan. This interaction was found to produce a specific analytical technique for tryptophan. Analysis of reaction mixtures revealed that a yellow chromophore was responsible for the production of absorbance with lDmax at 358 nm. Measurement of N‐terminal tryptophan dipeptides was successful whereas attempts to measure the tryptophan content of lysozyme and C‐terminal tryptophan dipeptides were unsuccessful utilizing this reaction.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
