Thin-layer chromatography of amino acids

Pataki, György

doi:10.1016/0009-5907(67)80007-3

Cited by 21 publications

(1 citation statement)

References 164 publications

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“…For developing the chromatograms, butanol/ acetic acid/water (4:1:1) (solvent A) was used in the first dimension, and phenol/water (75:25) (solvent B) was used in the second dimension (33). Amino acid standards were detected with ninhydrin reagent (0.3% in acetone); for development, the chromatogram was sprayed and heated at 60°C for 20 min.…”

Section: Fig 1 Spatial Organization Of the Functional Domains Inmentioning

confidence: 99%

Mapping and Molecular Modeling ofS-Adenosyl-l-methionine Binding Sites inN-Methyltransferase Domains of the Multifunctional Polypeptide Cyclosporin Synthetase

Velkov

Lawen

2003

Journal of Biological Chemistry

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We employed a highly specific photoaffinity labeling procedure, using 14 The modified sequence regions correspond to the motif II consensus sequence element, which is involved in directly complexing the adenine and ribose components of AdoMet. We conclude that the AdoMet binding to nonribosomal peptide synthetase N-methyltransferase domains obeys the consensus cofactor interactions seen among most structurally characterized low molecular weight AdoMet-dependent methyltransferases.

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Section: Fig 1 Spatial Organization Of the Functional Domains Inmentioning

confidence: 99%

Mapping and Molecular Modeling ofS-Adenosyl-l-methionine Binding Sites inN-Methyltransferase Domains of the Multifunctional Polypeptide Cyclosporin Synthetase

Velkov

Lawen

2003

Journal of Biological Chemistry

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Amino acid mixture analysis by mass spectrometry in the form of their dimethylaminomethylene methyl esters

Horman

Hesford

1974

Biol. Mass Spectrom.

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Abstrae-The amino acids, arginine. citrulline, cysteine, cystine, histidine, hydroxyproline, rnethionine. ornithine, proline. serine, threonine. tryptophan and tyrosine. have been analysed in the form of their N-(N',N'-dimethylaminomethylene) methyl esters. formed in a single step by reaction of the free amino acid or its hydrochloride with N,N-dimethylformamide dimethylacetal in acetonitrile/methanol (2 : 1). A reaction time of 15 minutes at 100 "C ensures complete derivatization, the derivatives being volatile at source ternperatures below 150 "C. and giving electron impact spectra characterized by abundant (or moderately abundant) peaks at or near the m a s of the molecular ion.The analysis of amino acid mixtures by mass frdgmentography on characteristic high m a s peaks of their N-(N',N'-dimethylaminoeth~lene) methyl ester derivatives. introduced on a direct insertion probe and volatilized during temperature programming of the source, is described. The method is applied to the analysis of a mixture containing arginine, citrulline, cystine, histidine and tryptophan. traditionally difficult to analyse by other methods. A recent p~b l i c a t i o n~~ has described the use of dimethylformamide dialkyl acetals as reagents for the preparation of volatile amino acid derivatives. These reagents provide several advantages, not the least of which is the simultaneous derivatization of both the amino and the carboxylic groups according to the following reaction : ~heir~dimethylaminomethylene/alk y1 ester (N-DMAM/ alk. ester) derivatives by gas chromatography. Hydroxyamino acids, it was suggested, might be analysed by gas chromatography after initial formation of the N-DMAM/alk. ester followed by protection of the hydroxyl group as its TMS (trimethylsilyl) derivative. To do this, however, sacrifices one of the ma.jor advantages in the use of these derivatives, namely their ease of quantitative preparation in a single step. In addition, the possibility of chromatographing DMAM/alk. ester derivatives of, for example, cystine, cysteine and arginine seems remote.We have therefore explored the possibility of the identification and semiquantitative estimation of amino acids by the simple fractionation of the N-DMAMI methyl esters directly in the source of the mass spectrometer. This fractionation technique is similar to that described by Majer and Boulton for the separation and identification of o-, m-and p-t~ramine,~' the main difference being that Majer and Boulton used isothermal source conditions, whereas this technique employs a temperature programming of the source to accommodate the range of volatilities encountered in the amino acid derivatives. We have observed that even for hydroxyamino acids, the derivatives are suitably volatile and give m a s spectra with prominent char-OCH, RCHCOOCH, 1 acteristic peaks. Good results were also obtained for arginine, citrulline and the thioamino acids, methionine,

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Rapid and quantitative blood amino acid analysis by chemical ionization mass spectrometry

Mee

Korth

Halpern

et al. 1977

Biol. Mass Spectrom.

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A quantitative analysis of amino acids in microsamples of dried blood spots by chemical ionization mass spectrometry has been developed. Isotope ratio determination was used as the quantitating technique via multiple labelled internal standards. This procedure yields excellent precision and accuracy as demonstrated by the analysis of known amino acid mixtures and of phenylalanine in the blood from newborns.

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Thin-layer chromatography of amino acids

Cited by 21 publications

References 164 publications

Mapping and Molecular Modeling ofS-Adenosyl-l-methionine Binding Sites inN-Methyltransferase Domains of the Multifunctional Polypeptide Cyclosporin Synthetase

Mapping and Molecular Modeling ofS-Adenosyl-l-methionine Binding Sites inN-Methyltransferase Domains of the Multifunctional Polypeptide Cyclosporin Synthetase

Amino acid mixture analysis by mass spectrometry in the form of their dimethylaminomethylene methyl esters

Rapid and quantitative blood amino acid analysis by chemical ionization mass spectrometry

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