Abstract
A method has been developed for determination of the specific radioactivity of l-leucine in different proteins or protein subunits which have been separated by polyacrylamide gel electrophoresis. After electrophoresis, the proteins are visualized by staining with Coomassie Brilliant Blue R, and the desired bands are excised and hydrolyzed with hydrochloric acid. In one aliquot of the hydrolysate, the radioactivity is determined, and in another, the amino acid concentration. For this purpose, we have employed an isotope dilution procedure, using the aminoacyl synthetase reaction. With this technique, 100–1500 picomol of a single amino acid can be detected.
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.
