Erythro-γ-hydroxyhomo-L-arginine: An amino acid from seed of Lonchocarpus costaricensis, and its preferential interaction with borate |
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| Authors: | Stephen V. Evans Linda E. Fellows Daniel H. Janzen John Chambers Robert C. Hider |
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| Affiliation: | 1. Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, U.S.A.;2. Ministry of Agriculture, Fisheries and Food, Slough Laboratory, London Road, Slough SL3 7HJ, U.K.;3. Department of Chemistry, University of Essex, Colchester CO4 3SQ, U.K. |
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| Abstract: | A new non-protein amino acid, erythro-γ-hydroxyhomo-L-arginine has been isolated from seed of Lonchocarpus costaricensis by exploiting its property of interacting with borate ions. For structural comparisons, threo-γ-hydroxyhomo-L-arginine was isolated from seed of Lathyrus tingitanus and erythro-γ-hydroxyarginine from Vicia unijuga by novel procedures. The reasons for the interaction of borate with the erythro- but not the threo-forms of these amino acids are discussed. |
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| Keywords: | Leguminosae non-protein amino acid borate complex. |
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