[Effect of cultivation conditions on the electrophoretic spectrum of various dehydrogenases in Saccharomyces cerevisiae].
The activity and electrophoretic spectrum of glucose-6-phosphate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase in Saccharomyces cerevisiae 14 depended on the conditions of cultivation, i. e. the sources of carbon and their concentration, the content of nitrogen, and aeration of the medium. A heterogeneous tris-buffer protein fraction was isolated after disintegration of the cells; the dehydrogenases were represented by several molecular forms whose number, electrophoretic mobility, and activity depended on the conditions of cultivation.
D000332:Aerobiosis; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D002244:Carbon / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism
D002244:Carbon; D000429:Alcohol Oxidoreductases; D008291:Malate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D009584:Nitrogen
Elektroforeticheskiĭ spektr nekotorykh degidrogenaz drozhzheĭ Saccharomyces cerevisiae v zavisimosti ot usloviĭ kul'tivirovaniia