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. 1967 Dec;42(12):1780-6.
doi: 10.1104/pp.42.12.1780.

Invertase inhibitor from potatoes: purification, characterization, and reactivity with plant invertases

R Pressey  1
Affiliations

Invertase inhibitor from potatoes: purification, characterization, and reactivity with plant invertases

R Pressey. Plant Physiol. 1967 Dec.

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 Cgamma 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.

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References

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