Probes of β-galactosidase structure with antibodies. Reaction of antipeptide antibodies against native enzyme

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Abstract
Antibodies were prepared against 18 tryptic and CNBr peptides from [Escherichia coli] .beta.-galactosidase [EC 3.2.1.23] ranging in size from 15-96 amino acid residues representing more than 80% of the polypeptide chain. They were tested for binding capacity and affinity toward their homologous antigens and toward the whole native protein. Nine antisera bound to .beta.-galactosidase; these were raised against certain peptides from the central and carboxyl-terminal regions of the polypeptide chain. Based on these results a preliminary model of the 3-dimensional structure of the folded protein is suggested.