Cetus Corporation

Sheng-Yung Chang

Arie Ben-Bassat

Shing Chang

Keith A Bauer

Method of obtaining N-terminal methionine-free proteins are described. The methods employ a novel enzyme, E. coli methionine aminopeptidase either in vitro or in vivo. For in vivo application, plasmid-borne DNA encoding the peptidase is transformed into a bacterial host which produces the desired protein.

Bacterial methionine n-terminal peptidase

Methods of obtaining N-terminal methionine-free proteins are described. The methods employ a novel enzyme, E. coli methionine aminopeptidase either in vitro or in vivo. For in vivo application, plasmid-borne DNA encoding the peptidase is transformed into a bacterial host which produces the desired protein.

Bacterial methionine N-terminal peptidase

Methods for obtaining N-terminal methionine-free proteins involve a novel E. coli methionine amino peptidase. The method is capable of in vitro or in vivo application. For in vivo application, a plasmid-borne DNA encoding the peptide is expressed in a bacterial host.

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Oakland, CA, United States of America

Sheng-Yung Chang