Abstract
As stated in a previous paper1, glutamic aminopherase from muscle tissue is absolutely specific for amino acids of the l-series. Slight trans-amination effects with the artificial d-amino acids (optically pure) in the presence of native muscle pulp, then considered as requiring additional proof, have since been observed almost regularly in some twenty-five experiments with d-glutamic acid and pyruvate or with d-alanine, d-valine, d-leucine and d-isoleucine and α-ketoglutarate. The mean ratio of the trans-amination values of the optical antipodes (l/d), computed from the experiments with glutamic acid and with alanine, amounts to 7·3 (Table 1).
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References
Braunstein, A. E., NATURE, 143, 609, (1939).
Kögl, F., and Erxleben, H., Z. physiol. Chem., 268, 57, (1939).
Euler, H., et al., Z. physiol. Chem., 259, 201, (1939).
Braunstein, A., and Kritzmann, M., Enzymologia, 2, 144, (1937).
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BRAUNSTEIN, A., AZARKH, R. Trans-amination of l- and d-Amino Acids in Normal Muscle and in Malignant Tumours. Nature 144, 669–670 (1939). https://doi.org/10.1038/144669a0
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DOI: https://doi.org/10.1038/144669a0
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