[Effect Of Polyelectrolytes on Catalytic Activity of Alcohol Dehydrogenase].
Fluorescent and optical spectroscopy were used to study the interaction of alcohol dehydrogenase (ADH) with negatively charged polystyrene sulfonate (PSS) and dextran sulfate (DS), as well as positively charged poly(diallyldimethylammonium) (PDADMA). As found, DS and PDADMA did not affect the structural and catalytic enzyme properties. In contrast, PSS slightly decreased the protein self-fluorescence over 1 h of incubation, which is associated with partial destruction of its quaternary (globular) structure. Investigation of the ADH activity with and without PSS showed its dependency on the incubation time and the PSS presence. Sodium chloride (2.0 M and 0.2 M) or ammonium sulfate (0.1 M) added to the reaction mixture did not completely protect the enzyme quaternary structure from the PSS action. However ammonium sulfate or 0.2 M sodium chloride stabilized the enzyme and partially inhibited the negative PSS effect.
A V
AV
Dubrovsky
E V
EV
Musina
A L
AL
Kim
S A
SA
Tikhonenko
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D016264:Dextran Sulfate / Q000737:chemistry*; D011095:Polyethylenes / Q000737:chemistry; D011137:Polystyrenes / Q000737:chemistry*; D017434:Protein Structure, Tertiary / Q000187:drug effects; D000644:Quaternary Ammonium Compounds / Q000737:chemistry
D011095:Polyethylenes; D011137:Polystyrenes; D000644:Quaternary Ammonium Compounds; C041004:poly-N,N-dimethyl-N,N-diallylammonium chloride; C003321:polystyrene sulfonic acid; D016264:Dextran Sulfate; D000426:Alcohol Dehydrogenase