Abstract
WORK from this laboratory has shown that transglutaminase catalyses the hydrolysis of the amide group of protein-bound glutamine, and its exchange with primary amines1. In addition, preliminary evidence indicated that the e-amino group of protein-bound lysine may act as a replacing amine2. Therefore, by the action of transglutaminase, various proteins can be modified and the new protein species may have properties unlike those of the original protein; for example, proteins may acquire novel antigenic properties as shown by proteins in which the e-amino group of lysine had been modified by substitution with polyamino-acids by chemical means3,4. Modifications produced enzymatically by the linkage of two proteins to each other through the γ-carboxyl group of protein-bound glutamic acid and the e-amino group of protein-bound lysine are of particular interest.
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.
