Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

L-Lactic Dehydrogenase from bovine heart has been used:as a reference standard to measure the LDH (lactic dehydrogenase)to quench protein-bound NADH in cellsto measure the lactate released by the cells in suspension

For use in enzymatic determination of lactate or pyruvate.

Biochem/physiol Actions

LDH (lactic dehydrogenase) helps in the reversible conversion oflactatetopyruvate.

Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.

General description

LDH (lactic dehydrogenase) is a glycolytic enzyme. It is found in skeletal muscle, heart, liver, kidneys, brain, lungs and red blood cells. It comprises of five isoenzyme forms. LDH possess a tetrameric structure.

Packaging

2.5 mL in glass bottle

Physical form

Suspension in 2.2 M ammonium sulfate

Unit Definition

One unit will reduce 1.0 µmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.