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The effect of heparin and pentosan polysulfate on the thermal stability of yeast alcohol dehydrogenase
Author(s) -
Paulíková Helena,
Molnárová Milota,
Podhradský Dusan
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800204432
Subject(s) - thermostability , chemistry , heparin , alcohol dehydrogenase , incubation , yeast , enzyme , thermal stability , biochemistry , chromatography , organic chemistry
Heparin and pentosan polysulfate as organic polyanions inhibit yeast alcohol dehydrogenase (YADH). The aim of this study was to determine the effect of heparin and pentosan polysulfate on the thermostability of alcohol dehydrogenase. Spectral and kinetic analyses showed that these compounds increase the thermal stability of the enzyme and eliminate entirely thermal aggregation. The thermostabilizing effect of unfractionated heparin and pentosan polysulfate was accelerated in the presence of NAD+. The addition of NAD+ (11 μM) to the incubation medium decreased the inhibition of the YADH activity in the presence of pentosan polysulfate (1.32 μM). Moreover, 38 % of the residual activity of YADH was found after a 5‐rain incubation at 70 °C. These findings indicate that heparinoids not only modulate the enzyme activity but also can prevent the protein's thermal denaturation.