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Identification of N-terminal amino acids in the form of fluorescent thiohydantoins

✍ Scribed by Zdeněk Deyl

Publisher
Elsevier Science
Year
1970
Tongue
English
Weight
497 KB
Volume
48
Category
Article
ISSN
1873-3778

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✦ Synopsis

Out of three different types of aromatic isothiocyanates tested, x-naphthylisothiocyanate is the most suitable for stepwise degradation of proteins. The hydantoins formed exhibit good chromatographic properties on paper (solvents : 5% acetic acid; 10% pyridine; phosphate buffer, pH 6, ,u 0.1) and on electrophoresis (pyridineacetate buffer). The pH dependence of the emitted fluorescence, which differs for individual amino acids, is of great diagnostic value. The sensitivity is due to the luminescent properties of these derivatives being increased up to the order IO-" to ro-4 pmoles, which is comparable to the sensitivity of the x-dimethylamino-5naphthalene sulphochloride (DANSY L) derivatives.

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Quantitative protein sequencing using mass spectrometry: thermally induced formation of thiohydantoin amino acid derivatives from N-methyl- and N-phenylthiourea amino acids and peptides in the mass spectrometer
✍ T. Fairwell; S. Ellis; R.E. Lovins 📂 Article 📅 1973 🏛 Elsevier Science 🌐 English ⚖ 365 KB

The thermally induced formation of methyl-and phenylthiohydantoin amino acid derivatives from the corresponding N-methyl-and N-phenylthiourea derivatives of amino acids and peptides has been shown to occur in the mass spectrometer. A comparison of the mass spectra of a number of amino acid thiourea