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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Bibliographic Details
Published inAnalytical biochemistry Vol. 12; no. 1; pp. 36 - 40
Main Author Davis, Leodis
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.07.1965
Subjects
Animals
Biological Assay
Butyrates - metabolism
Hydro-Lyases - metabolism
In Vitro Techniques
Keto Acids - metabolism
Liver - enzymology
Pyruvates - metabolism
Sheep
Spectrophotometry
Threonine - metabolism
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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.
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