title: Effect of ozone on ATP, cytosolic enzymes and permeability of Saccharomyces cerevisiae.
abstract: Treatment of a yeast suspension with ozone inactivates a number of cytosolic enzymes. Among 15 studied, the most drastic inactivation was found for glyceraldehyde-3-phosphate dehydrogenase and to lesser extents: NAD-glutamate dehydrogenase, pyruvate decarboxylase, phosphofructokinase-1 and NAD-alcohol dehydrogenase. Ozone treatment also effects the quantity of ATP and of other nucleoside triphosphates, reducing to about 50% of the initial value. The ATP missing in the cells appears in the medium. NAD and protein also accumulate in the medium suggesting that the yeast cells have been permeabilized. Permeabilization of the yeast cells by treatment with ozone precedes the inactivation of glyceraldehyde-3-phosphate dehydrogenase and other cytosolic enzymes.
authors.forename: H
authors.initials: H
authors.lastname: Hinze
authors.forename: D
authors.initials: D
authors.lastname: Prakash
authors.forename: H
authors.initials: H
authors.lastname: Holzer
mesh_terms: D000244:Adenosine Diphosphate / Q000032:analysis; D000255:Adenosine Triphosphate / Q000032:analysis*; D002463:Cell Membrane Permeability / Q000187:drug effects*; D003600:Cytosol / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000032:analysis; D010126:Ozone / Q000633:toxicity*; D012441:Saccharomyces cerevisiae / Q000032:analysis / Q000187:drug effects*
chemical_list: D000244:Adenosine Diphosphate; D010126:Ozone; D000255:Adenosine Triphosphate; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases