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Etude de structures peptidiques à l'aide de phénylisothiocyanate IV. Note sur la préparation et la purification des phénylthiohydrantoïnes dérivées de divers acides aminés

✍ Scribed by Emile Cherbuliez; J. Marszalek; J. Rabinowitz

Publisher
John Wiley and Sons
Year
1963
Tongue
German
Weight
257 KB
Volume
46
Category
Article
ISSN
0018-019X

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✦ Synopsis

Abstract

The authors describe modified procedures for the synthesis of phenylthiohydantoins derived from α‐amino acids, applied to 16 amino acids. With the exception of the phenylthiohydantoins containing a free NH~2~, CONH~2~, COOH or hetero‐cyclic group belonging to the starting amino acid, they can be purified by sublimation. The yield of chromatographically pure product vary between 54 yo (threonine) and 92% (tyrosin); with asparagine, the yield did not exceed 49%.

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Etude de structures peptidiques à l'aide
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## Abstract Using a solution of [^35^S]‐phenylisothiocyanate in pentane with a specific activity of 30 to 8O mC/mmole, the authors have determined the sequence of di‐, tri‐peptides and a pentapeptide on the following quantities: 1 to 2 nmole of peptide when the [^35^S]‐phenylthiohydantoines obtaine

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By the analysis of di‐, tri‐peptides and a pentapeptide of known constitution the authors show that using an N,N‐dimethylformamide solution of [^35^S]‐phenylisothiocyanate with a spectific activity of 10 to 40 mc/mmole the sequence of amino acids can be determined starting with 0,005 micromole of pe

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## Abstract The microchromatography of phenylthiohydantoins on thin layers of silica (solvent: heptane, pyridine, ethyl acetate 5:3:2 vol.; revelation by starch‐iodineazide) is described. This method is 10 to 20 times more sensitive than that of classic paper chromatography. Good results are obtain