Chemical Forums
Specialty Chemistry Forums => Biochemistry and Chemical Biology Forum => Topic started by: hpl912 on August 03, 2008, 04:09:24 PM
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in performing assays of alpha ketoglutarate and pyruvate in sample mixtures, glutamate dehydrogenase and lactate dehydrogenase was used, respectively.
before the assay, samples were left incubated for 45 minutes at room temperature.
The question is, why it takes such longtime for the reactions to take place for the assay to give a correct / expected absorbance? If it was measured too fast after preparing, it gives a pretty different absorbance.
isn't this reaction kind of instantaneous? or is it because these reactions are going on the reversed unfavourable path so it must take longer for a complete reaction?
by reverse i mean by glutamate is catalyzed by GDH into alpha-KG + ammonia and alanine catalyzed by LDH to give pyruvate