The kinetics of diastereomeric amino acids with o‐phthaldialdehyde
Identifieur interne : 002042 ( Main/Exploration ); précédent : 002041; suivant : 002043The kinetics of diastereomeric amino acids with o‐phthaldialdehyde
Auteurs : Marc W. Meyer [Suisse] ; Veronika R. Meyer [Suisse] ; Stephan Ramseyer [Suisse]Source :
- Chirality [ 0899-0042 ] ; 1991.
English descriptors
- Teeft :
- Acid, Ambient temperature, Amino, Amino acid, Amino acid analysis, Amino acid epimers, Amino acid racemization, Amino acids, Chemical properties, Epimers, Fluorescence detection, Fluorescence properties, Indole, Indole reaction product, Isoleucine, Kinetics, Liquid chromatography, Mercaptoethanol, Organic chemistry, Postcolumn reaction detection, Protein hydrolysis, Racemization, Rate constants, Reaction kinetics, Reaction rate, Reaction temperature, Reaction time, Reagent, Snail shell samples, Ultrapure water, Worst case.
Abstract
The kinetics of the reaction of the amino acid epimers L‐isoleucine, D‐alloisoleucine, L‐threonine, and D‐allo‐threonine with o‐phthaldialdehyde and mercaptoethanol were determined at 25°C. L‐Isoleucine reacts faster than its D‐epimer whereas L‐threonine reacts slightly slower than its D‐epimer. In the case of isoleucine, the consequence can be an allo/iso ratio which in the worst case is 25% too low if these amino acids are quantified by liquid chromatography and o‐phthaldialdehyde fluorescence detection. The effect on dating of fossils by amino acid racemization is discussed.
Url:
DOI: 10.1002/chir.530030611
Affiliations:
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Le document en format XML
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<term>Amino acid</term>
<term>Amino acid analysis</term>
<term>Amino acid epimers</term>
<term>Amino acid racemization</term>
<term>Amino acids</term>
<term>Chemical properties</term>
<term>Epimers</term>
<term>Fluorescence detection</term>
<term>Fluorescence properties</term>
<term>Indole</term>
<term>Indole reaction product</term>
<term>Isoleucine</term>
<term>Kinetics</term>
<term>Liquid chromatography</term>
<term>Mercaptoethanol</term>
<term>Organic chemistry</term>
<term>Postcolumn reaction detection</term>
<term>Protein hydrolysis</term>
<term>Racemization</term>
<term>Rate constants</term>
<term>Reaction kinetics</term>
<term>Reaction rate</term>
<term>Reaction temperature</term>
<term>Reaction time</term>
<term>Reagent</term>
<term>Snail shell samples</term>
<term>Ultrapure water</term>
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<front><div type="abstract" xml:lang="en">The kinetics of the reaction of the amino acid epimers L‐isoleucine, D‐alloisoleucine, L‐threonine, and D‐allo‐threonine with o‐phthaldialdehyde and mercaptoethanol were determined at 25°C. L‐Isoleucine reacts faster than its D‐epimer whereas L‐threonine reacts slightly slower than its D‐epimer. In the case of isoleucine, the consequence can be an allo/iso ratio which in the worst case is 25% too low if these amino acids are quantified by liquid chromatography and o‐phthaldialdehyde fluorescence detection. The effect on dating of fossils by amino acid racemization is discussed.</div>
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