Abstract
β-Amylase from six-day-germinated maize grains was isolated by ammonium sulphate precipitation, chromatofocusing and adsorption chromatography on hydroxyapatite. The purification was followed by isoelectric focusing and SDS-PAGE, allowing a more than 400-fold enrichment in β-amylase. The maize enzyme is constituted of two isoforms with very close isoelectric points (4.25 and 4.40) and M r ca 65 000. Polyclonal antibodies were raised in rabbits and tested by immunoelectrophoresis and immunoblotting. They are monospecific for maize β-amylase and recognized the two isoforms as a single antigen. A faint cross reactivity with the sorghum enzyme was observed, but not with the barley or rice β-amylases.
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