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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