Abstract
A method for the structural analysis of Bence-Jones proteins has been devised. These proteins are isolated from the urine of patients with multiple myeloma by ammonium sulphate fractionation. The Bence-Jones proteins are reduced with mercapto-ethanol, amino-ethylated and purified by gel filtration on columns of Sephadex G-100. The purified Bence-Jones proteins are digested with trypsin and analysed by finger-printing. This method of analysis allows us to compare a large number of proteins. Proteins of immunological type K give fingerprints completely different from those of proteins of immunological type L. The method of analysis used allows us to establish the number of cysteine and tryptophan residues present in Bence-Jones proteins. Type L proteins show in fingerprints more tryptophan-containing peptides than type K proteins.
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.
