Enzymatic determination of carbon-14 labeled L-alanine in biological samples
A method for determination of L-alanine-specific radioactivity in biological samples is presented. This method is based on the specific enzymatic transformation of L-alanine to pyruvic acid hydrazone catalyzed by the enzyme L-alanine dehydrogenase, formation of the pyruvic acid 2,4-dinitrophenylhydrazone derivative, and quantitative trapping in Amberlite XAD-7 columns, followed by radioactivity counting of the lipophilic eluate. No interferences from other UC-labeled materials such as D-glucose, glycerol, L-lactate, L-serine, L-glutamate, L-phenylalanine, glycine, L-leucine, and L-arginine were observed. This inexpensive and high-speed method is applicable to the simultaneous determination of L-alanine-specific radioactivity for a large number of samples.
- Research Organization:
- Universitat de Les Illes Balears, Spain
- OSTI ID:
- 6426178
- Journal Information:
- Anal. Chem.; (United States), Vol. 59:14
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
ALANINE-L
CHEMICAL REACTIONS
LABELLED COMPOUNDS
BIOLOGICAL MATERIALS
QUANTITATIVE CHEMICAL ANALYSIS
CARBON 14
ACTIVITY LEVELS
CHEMICAL REACTION YIELD
ENZYMES
EXPERIMENTAL DATA
ALANINE-ALPHA
ALANINES
AMINO ACIDS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBON ISOTOPES
CARBOXYLIC ACIDS
CHEMICAL ANALYSIS
DATA
EVEN-EVEN NUCLEI
INFORMATION
ISOTOPES
LIGHT NUCLEI
MATERIALS
NUCLEI
NUMERICAL DATA
ORGANIC ACIDS
ORGANIC COMPOUNDS
RADIOISOTOPES
YEARS LIVING RADIOISOTOPES
YIELDS
400102* - Chemical & Spectral Procedures
400101 - Activation
Nuclear Reaction
Radiometric & Radiochemical Procedures