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- Title
Purification and Properties of Rape Alcohol Dehydrogenase.
- Authors
Leblová, Sylva; Stiborová, Marie
- Abstract
Germinating seeds with the highest specific activity (24 hour germination) were used for isolation of alcohol dehydrogenase, ADH, from rape (Brassica napus L. cv. Třebičská). The rape ADH was purified by fractionation with ammonium sulphate, desalting on Sephadex G-25, Chromatography on DEAE-cellulose and gel filtration on Sephadex G-25, chromatography on DEAE-cellulose and gel filtration on Sephadex G-150. Using this isolation procedure, enzyme with a specific activity 85.6 times higher than that of the crude extract was obtained. The molecular weight of the enzyme obtained is 66,000. The enzyme is a metallo-enzyme containing sulfhydryl groups as evidence by the inhibitory effect of chelating compounds and thiol reagents. The optimum pH for the oxidation of ethanol is 8.5 and for reduction of acetaldehyde 7.0. The enzyme exhibits a relatively wide substrate specificity towards alcohols. Dimethyl-sulphoxide (DMSO), some amides and oximes and some intermediates of the carbohydrate metabolism act as ADH inhibitors, ATP as analogue of NAD also exhibits an inhibitory effect. The inhibitory effect of heterocyclic substances (pyrazol, imidazol, pyridine) is similar to the effect on liver alcohol dehydrogenase.
- Subjects
SEED viability; GERMINATION; CHROMATOGRAPHIC analysis; CELLULOSE; MOLECULAR weights; HYDROGEN-ion concentration
- Publication
Physiologia Plantarum, 1976, Vol 38, Issue 3, p176
- ISSN
0031-9317
- Publication type
Article
- DOI
10.1111/j.1399-3054.1976.tb03986.x