Invertase Inhibitor from Potatoes: Purification, Characterization, and Reactivity with Plant Invertases
Open Access
- 1 December 1967
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 42 (12), 1780-1786
- https://doi.org/10.1104/pp.42.12.1780
Abstract
Invertase inhibitor was extracted from potato tubers and purified nearly 1000-fold. The purification procedure involved precipitation at pH 4.0, fractionation with ammonium sulfate, adsorption on alumina Cγ gel, and gel filtration on Sephadex G-100 and DEAE-Sephadex A-50. The product obtained was homogeneous to electrophoresis on polyacrylamide gel. Exclusion chromatography on Sephadex G-100 indicated a molecular weight of about 17,000. The inhibitor did not inhibit yeast, Neurospora, and several plant invertases. It completely inhibited potato tuber invertase and a number of other plant invertases. Some plant invertases were partially inhibited.This publication has 11 references indexed in Scilit:
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