Processing of a 58 × 10 3Mr invertase from potato tubers

Abstract

Processing of a 58 × 10 3 M r acid invertase to a 48 × 10 3 M r polypeptide has been demonstrated in potato tuber extracts using antibodies raised against a synthetic N-terminal peptide. Processing of the 58 × 10 3 M r protein occurred during the preparation of extracts in acetate buffer, pH 5.2, but not in Tris-HCI buffer, pH 7.5. A modified rapid extraction procedure suggested that the processing event also occurred in planta. Processing apparently increased the activity of acid invertase after foaming, a technique previously reported to dissociate the potato tuber invertase from an endogenous inhibitor. Western blot analysis revealed that the relative abundance of the 48 × 10 3 M r polypeptide was correlated with acid invertase activity.