Tryptophan analysis simultaneously with other amino acids in gas phase hydrochloric acid hydrolyzates using the Pico-TagTM Work Station

I. Molnár-Perl, M. Khalifa

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Classical liquid phase hydrolysis of proteins with hydrochloric acid in the presence of tryptamine [3-(2-aminoethyl)indole] has shown that tryptophan can be protected from destruction. An exhaustive study has been made to establish the optimum conditions for protein hydrolysis, in the gas phase using the Pico-TagTM Work Station, as a function of time and temperature. The amino acid content, including tryptophan and cyst(e)ine, of standard proteins such as lysozyme, human albumin and α-chymotrypsin were determined as phenylthiocarbamyl (PTC) derivatives. On 5 μm Hypersil columns (15×4.6 mm) the quantitation of twenty PTC amino acids requires 22 minutes. The reproducibility of the measurements was 5.8% (relative standard deviation) or less.

Original languageEnglish
Pages (from-to)43-46
Number of pages4
JournalChromatographia
Volume36
Issue number1
DOIs
Publication statusPublished - Dec 1993

Fingerprint

Hydrochloric Acid
Tryptophan
Gases
Amino Acids
Hydrolysis
Proteins
Chymotrypsin
Muramidase
Cysts
Albumins
Derivatives
Temperature
Liquids
tryptamine

Keywords

  • Acid hydrolysis after tryptamine treatment
  • Column liquid chromatography
  • Gas phase hydrolysis of proteins
  • PTC-amino acids
  • Tryptophan quantitation

ASJC Scopus subject areas

  • Analytical Chemistry
  • Clinical Biochemistry

Cite this

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abstract = "Classical liquid phase hydrolysis of proteins with hydrochloric acid in the presence of tryptamine [3-(2-aminoethyl)indole] has shown that tryptophan can be protected from destruction. An exhaustive study has been made to establish the optimum conditions for protein hydrolysis, in the gas phase using the Pico-TagTM Work Station, as a function of time and temperature. The amino acid content, including tryptophan and cyst(e)ine, of standard proteins such as lysozyme, human albumin and α-chymotrypsin were determined as phenylthiocarbamyl (PTC) derivatives. On 5 μm Hypersil columns (15×4.6 mm) the quantitation of twenty PTC amino acids requires 22 minutes. The reproducibility of the measurements was 5.8{\%} (relative standard deviation) or less.",
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N2 - Classical liquid phase hydrolysis of proteins with hydrochloric acid in the presence of tryptamine [3-(2-aminoethyl)indole] has shown that tryptophan can be protected from destruction. An exhaustive study has been made to establish the optimum conditions for protein hydrolysis, in the gas phase using the Pico-TagTM Work Station, as a function of time and temperature. The amino acid content, including tryptophan and cyst(e)ine, of standard proteins such as lysozyme, human albumin and α-chymotrypsin were determined as phenylthiocarbamyl (PTC) derivatives. On 5 μm Hypersil columns (15×4.6 mm) the quantitation of twenty PTC amino acids requires 22 minutes. The reproducibility of the measurements was 5.8% (relative standard deviation) or less.

AB - Classical liquid phase hydrolysis of proteins with hydrochloric acid in the presence of tryptamine [3-(2-aminoethyl)indole] has shown that tryptophan can be protected from destruction. An exhaustive study has been made to establish the optimum conditions for protein hydrolysis, in the gas phase using the Pico-TagTM Work Station, as a function of time and temperature. The amino acid content, including tryptophan and cyst(e)ine, of standard proteins such as lysozyme, human albumin and α-chymotrypsin were determined as phenylthiocarbamyl (PTC) derivatives. On 5 μm Hypersil columns (15×4.6 mm) the quantitation of twenty PTC amino acids requires 22 minutes. The reproducibility of the measurements was 5.8% (relative standard deviation) or less.

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