Abstract
WHILE investigating the specificity of acylase activity of soil bacteria on acyl derivatives of aminoacids1–3, we noted that the acetone powder of Ehrlich ascites carcinoma cells was able to hydrolyse dichloro-acetyl-DL-aspartic acid but not (or only to a small extent) the dichloroacetyl derivatives of some aminoacids such as DL-glutamic acid, DL-serine, DL-methionine and DL-phenylalanine4.
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Kameda, Y., et al., Nature, 169, 1016 (1952); 170, 888 (1952); 181, 1225 (1958); 182, 453 (1958).
Kameda, Y., et al., Yakugaku Zasshi, 78, 202, 748, 754, 759, 763, 765, 767, 769 (1958); 80, 362 (1960).
Kameda, Y., et al., Chem. Pharm. Bull., 6, 321, 394, 395, 441 (1958); 7, 702, 785, 787, 789 (1959).
Kameda, Y., Toyoura, E., Kimura, Y., Matsui, K., Omori, T., and Takeuchi, K., Yakugaku Zasshi, 77, 1351 (1957).
Kameda, Y., et al., Chem. Pharm. Bull. (in the press).
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KAMEDA, Y., MATSUI, K., KIMURA, Y. et al. Acylase Activity of Ascites Tumour Cells on Dichloroacetyl Derivatives of Amino-acids. Nature 192, 468 (1961). https://doi.org/10.1038/192468a0
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DOI: https://doi.org/10.1038/192468a0
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