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pubmed:abstractText |
1. Penicillin amidase from Proteus rettgeri was purified 580-fold by a four-step chromatographic procedure. Titration with phenylmethanesulphonyl fluoride showed that the purified preparation contains 53% of the enzyme. 2. The molecular weight of the amidase was found to be 65.000. The enzyme is strongly inhibited by N-bromosuccinimide and zinc ions. It hydrolyses penicillins, cephalosporins and some synthetic substrates, and in addition it catalyses synthesis of ampicillin from methyl ester of phenylglycine and 6-aminopenicillanic acid. 3. The immobilized amidase obtained by copolymerization of the chemically modified enzyme with acrylamide was applied for preparative hydrolysis of benzylpenicillin.
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