Literature DB >> 6336371

Resolution of amino acids by a native-cellulose column.

S Yuasa1, M Itoh, A Shimada.   

Abstract

Seventeen aliphatic, hydroxyl, sulfur-containing, aromatic, imino, and heterocyclic DL-amino acids were resolved without derivatization using a native-cellulose column. Chirality was assigned by either CD spectra or co-chromatography. Under these conditions, it is known that the hydrophobic interaction of amino acids with the hydroxyl groups on the cellulose played an important role in the separations. The cellulose column chromatographic system for resolution of amino acid enantiomers was combined with an amino acid analyzer. Thus, the DL-amino acids separated by the latter system were successively resolved by the former.

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Year:  1984        PMID: 6336371     DOI: 10.1093/chromsci/22.7.288

Source DB:  PubMed          Journal:  J Chromatogr Sci        ISSN: 0021-9665            Impact factor:   1.618


  3 in total

1.  Tryptophanase-catalysed degradation of D-tryptophan in highly concentrated diammonium hydrogen phosphate solution.

Authors:  A Shimada; H Shishido; I Nakamura
Journal:  Amino Acids       Date:  1996-03       Impact factor: 3.520

2.  Couplings of character and of chirality in the origin of the genetic system.

Authors:  J C Lacey; N S Wickramasinghe; G W Cook; G Anderson
Journal:  J Mol Evol       Date:  1993-09       Impact factor: 2.395

3.  Tryptophanase-catalyzed L-tryptophan synthesis from D-serine in the presence of diammonium hydrogen phosphate.

Authors:  Akihiko Shimada; Haruka Ozaki; Takeshi Saito; Fujii Noriko
Journal:  Int J Mol Sci       Date:  2009-06-03       Impact factor: 6.208

  3 in total

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