title: Effects of trehalose on pressure-induced inactivation of yeast alcohol dehydrogenase.
abstract: Isozymes of yeast alcohol dehydrogenase are slowly denatured at moderate hydrostatic pressures (<3 kbar). The time courses for inactivation are biphasic and both phases of both isozymes are protected by trehalose. ADH-I is slightly more barostable than ADH-II which is opposite to their thermostabilities. Trehalose at 1M extends their half-lives about 6-fold at 2 kbar, pH 7.5 and 25 degrees C. In contrast, 1M sucrose provides only 4.4-fold protection under identical conditions, a finding consistent with the superior protein stabilization of trehalose to other denaturants.
authors.affiliation: Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705, USA.
authors.forename: Hyun
authors.initials: H
authors.lastname: Park
authors.forename: Gene
authors.initials: G
authors.lastname: Kidman
authors.forename: Dexter B
authors.initials: DB
authors.lastname: Northrop
mesh_terms: D000426:Alcohol Dehydrogenase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability; D006874:Hydrostatic Pressure; D007700:Kinetics; D011489:Protein Denaturation / Q000187:drug effects; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014199:Trehalose / Q000494:pharmacology*
chemical_list: D014199:Trehalose; D000426:Alcohol Dehydrogenase