| Literature DB >> 6405659 |
Abstract
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 be pH 7.0 and the Km value for dopa was determined to be 4 X 10(-5) M.Entities:
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Year: 1983 PMID: 6405659 DOI: 10.1016/0003-2697(83)90570-5
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365