Uric acid substantially enhances the free radical-induced inactivation of alcohol dehydrogenase.

Abstract:

:Lactate dehydrogenase (LDH) and yeast alcohol dehydrogenase ( YADH ) are inactivated when attacked by hydroxy free radicals (OH). Organic molecules with a high rate constant of reaction with OH such as ascorbate or urate can compete with the enzymes for these strongly oxidising radicals. However, although 10(-3)M ascorbate can substantially protect both LDH and YADH from OH attack, in the presence of 10(-3)M urate only LDH is protected. In the case of YADH an even greater degree of inactivation than with OH occurs. The extent of inactivation is considerably reduced when oxygen is absent, in agreement with a urate peroxy radical perhaps being partly responsible for the increased inactivation of the enzyme.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kittridge KJ,Willson RL

doi

10.1016/0014-5793(84)81391-5

subject

Has Abstract

pub_date

1984-05-07 00:00:00

pages

162-4

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(84)81391-5

journal_volume

170

pub_type

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