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High‐pressure enzyme kinetics
Author(s) -
Chernyak V.Ya.,
Drachev V.A.,
Nikolaeva N.G.,
Chernyak B.V.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80296-3
Subject(s) - kinetics , lactate dehydrogenase , chemistry , pyruvate dehydrogenase complex , reaction rate constant , enzyme , pyruvate dehydrogenase kinase , pyruvate dehydrogenase phosphatase , pyruvate decarboxylation , reaction rate , dehydrogenase , biochemistry , stereochemistry , catalysis , physics , quantum mechanics
A newly designed optical cell allows an enzyme reaction to be started under high pressure and makes it possible to begin measurement of the reaction rate after a ‘dead time’ no longer than 1–2 s. This device was used to study the kinetics of lactate dehydrogenase reaction at 1 kbar. At this pressure lactate dehydrogenase from rabbit muscle exhibited a rapid deactivation in the presence of NADH if pyruvate was absent. After addition of pyruvate the reaction was initiated and proceeded at a constant rate, i.e., without loss of enzyme activity. It is suggested that pyruvate markedly increases the association constant of this tetrameric enzyme.