The nonenzymatic decarboxylation of dopa was completely blocked by both 2-mercaptoethanol and EDTA together over the wide range of pH. This finding made it possible to measure the activity of dopa decarboxylase precisely even at an alkaline pH value. The pH optimum of dopa decarboxylase was found to
β¦ LIBER β¦
Inhibition of DOPA decarboxylation by analogues of tryptophen
β Scribed by Talmage R. Bosin; John R. Baldwin; Roger P. Maickel
- Book ID
- 115774192
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 392 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0006-2952
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