Abstract
Supernatant malate dehydrogenase, treated with tritiated coenzyme (NAD- αβ 3H) or substrate (DL-malic-2- 3H) in a manner similar to other dehydrogenases (1–4), coprecipitates tightly bound tritiated coenzyme when perchloric acid is added. Nearly all of the radioactivity is removed by dialysis. A very small amount of covalently bound tritium is found in tryptophan-containing peptides.
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