Invertase Inhibitor from Potatoes: Purification, Characterization, and Reactivity with Plant Invertases | Zendy

Russell Pressey | Zendy

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Invertase Inhibitor from Potatoes: Purification, Characterization, and Reactivity with Plant Invertases

Author(s) -

Russell Pressey

Publication year - 1967

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.42.12.1780

Subject(s) - sephadex , invertase , size exclusion chromatography , ammonium sulfate precipitation , chromatography , polyacrylamide gel electrophoresis , chemistry , biochemistry , fractionation , ammonium , biology , enzyme , organic chemistry

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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