Abstract

Mouse monoclonal antibodies were prepared against β-galactosidase (EC 3.2.1.23) of Escherichia coli. The binding sites of these monoclonal antibodies within the β-galactosidase molecule were estimated by immunoblot analyses to various defined peptide regions of β-galactosidase, encoded by expression plasmids. Monoclonal antibodies, were characterised, which either bind to the amino-terminal or to the carboxy-terminal region or to an internal section of β-galactosidase. These defined monoclonal antibodies were shown to be a useful tool for characterisation of β-galactosidase fusion proteins expressed in Escherichia coli. Galactosidase, β-; Monoclonal antibody; Recombinant expression product; Epitope mapping; ( E. coli)

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