Cellulose conformation responsible for resolution of DL-amino acids |
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Authors: | S. Yuasa A. Shimada M. Isoyama T. Fukuhara M. Itoh |
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Affiliation: | (1) Department of Biology, College of General Education, Osaka University, 560 Toyonaka, Osaka, Japan |
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Abstract: | Summary For the purpose of biochemical study, the resolution of non-derivatized DL-amino acids was carried out by using native-cellulose thin-layer and column chromatography. Its resolution capability was known to be in proportion to the increase of environmental hydrophobicity. It is suggested that the resolutions of DL-amino acids might be resulted from the cellulose conformation change under hydrophobic conditions. The model structures of cellulose are proposed in order to understand the mechanism of chiral selection of amino acids on its molecular surface. LEB/OU contribution No. 70 |
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Keywords: | Thin-layer chromatography Column liquid chromatography Cellulose conformation Hydrophobicity DL-amino acids |
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