Abstract
A general method for the isolation of modified tryptophan-containing peptides is described, which takes advantage of the adsorption properties of tale for aromatic nitrocompounds. The method has been extensively assayed on tryptic and chymotryptic hydrolyzates of human Bence Jones proteins of k and λ type and of human serum albumin, and in preliminary experiments on egg white lysozyme and rabbit IgG light chains. All those proteins had been previously carboxymethylated and modified with 2,4 dinitrophenylsulfenylchloride, a selective reagent for tryptophan.
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 callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
