Showing papers on "Penicillin amidase published in 1972"

TL;DR: The enzyme was shown to be inhibited by excess substrate, benzylpenicillin, and by both of the products of hydrolysis, which was found to be competitive and by 6-aminopenicillanic acid to be non-competitive.

TL;DR: Penicillin amidase has been immobilised by covalent binding to DEAE-cellulose using 2-amino-4,6-dichloro-s-triazine and there was no evidence of diffusional limitation of the reaction rate.