A spectrophotometric method for the assay of threonine dehydratase
The enzymic conversion of β-hydroxy α-amino acids to α-keto acids by ThrDH (sheep liver) was followed by a direct spectrophotometric method at 230 mμ. The assay was more sensitive to changes in keto acid concentrations than the 2,4-dinitrophenylhydrazone method because of the absence of the high and...
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Published in | Analytical biochemistry Vol. 12; no. 1; pp. 36 - 40 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.07.1965
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Subjects | |
Online Access | Get full text |
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Summary: | The enzymic conversion of β-hydroxy α-amino acids to α-keto acids by ThrDH (sheep liver) was followed by a direct spectrophotometric method at 230 mμ. The assay was more sensitive to changes in keto acid concentrations than the 2,4-dinitrophenylhydrazone method because of the absence of the high and variable blanks of the latter method. However, in the applicable range of concentrations both methods gave the same results. This procedure is not handicapped by the physical properties inherent in the coupled reactions. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0003-2697 1096-0309 |
DOI: | 10.1016/0003-2697(65)90139-9 |