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Interactions between heparinoids and alcohol dehydrogenase
Author(s) -
Paulíková Helena,
Valusová Eva,
Antalík Marián
Publication year - 1997
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 - 10.1080/15216549700203081
Subject(s) - chemistry , nad+ kinase , alcohol dehydrogenase , ionic strength , enzyme , yeast , polysaccharide , heparin , ethanol , fluorescence , alcohol , biochemistry , chromatography , nuclear chemistry , organic chemistry , aqueous solution , physics , quantum mechanics
The interaction between polysulfated polysaecharides (low‐molecular‐weight heparin LMWH, dextran sulfate DS and pentosan sulfate PS) and yeast alcohol dehydrogenase (YADH) was investigated. The fluorescence and UV spectra of YADH after adding the tested polysaccharides have confirmed the interaction between the enzyme and these compounds. Kinetic studies have shown that LMWH, DS and PS are inhibitors of YADH (mixed type with respect to NAD). The most potent inhibitor is PS (ID50=37.5 ng/ml, Ki=0.6 μM). The inhibition effect depends on the ionic strength (the inhibition decreased by about 50% in the presence of 100 mM Na2SO4) and pH value (the inhibition decreased at pH>7). The results indicate that the inhibition effect of these polyanions is caused by their electrostatic interactions with the NAD‐binding region of YADH.