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.
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