Abstract
It was found that the paper electrophoretic method is useful in the detection of amines formed by the decarboxylation of amino acids. Using Escherichia coli No.1, arginine and its structurally allied compound, canavanine, were decomposed and the products were submitted to electrophoresis. By coloration with the Sakaguchi and nitroprusside reaction, agmatine was detected from arginine, and a new substance, possessing o-guanidyl group, with stronger basicity than the parent compound, was obtained from canavanine. Its structure was presumed from the distance of its migration. Decomposition of arginine and canavanine was examined with Staphylococcus aureus 209 P, Lactobacillus 17-5, and Streptococcus fecalis R, and found that the decomposition was effected in all the cases without decarboxylation. The present method was also used in examining the activity of decarboxylase of amino acids with E. coli No.1, and it was found that the decarboxylation was effected with arginine, canavanine, lysine, glutamic acid, histidine, and ornithine, while this bacillus did not have any ability of decarboxylating canarine, tyrosine, tryptophan, phenylalanine, leucine, serine, threonine, aspartic acid, citrulline, diaminobutyric acid, valine, alanine, and DOPA.
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