コリスチン関連化合物の研究(第4報) : モノDNP-コリスチンおよびDNP-コリスチンメタンスルホン酸ソーダの加水分解について

概要

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Since sodium colistinmethansulfonate (1) gives the positive colour reaction of the primary amines, the existence of free amino radical in its molecule is suggested. In order to investigate the differences of five amino radicals in colistin, (1) was dinitrophenylated with dinitrofluorobenzene (DNFB) and the dinitrophenylated-1 was hydrolyzed with HCl to afford six partial peptides. The arrangements of amino acids were decided by the determination of the composition of amino acids, C-terminal amino acids and N-terminal amino acids in each peptide. The γ-amino radical of diaminobutyric acid next to L-leucine was proved to be dinitrophenylated. On the other hand, colistin sulfate and colistin base were mono-dinitrophenylated with one molar DNFB and the consequent DNP-colistin was partially hydrolyzed. The arrangements of the amino acids of these partial peptides were decided by the same method as in (1). 6-methyl-octanoic acid was found by gas chromatography in all these peptides. From these data, it is assumed that the γ-amino radical of the terminal diaminobutyric acid in the side chain tripeptide would be the most reactive radical and the γ-amino radical of the diaminobutyric acid adjoining L-leucine would be the most inactive amino radical in the colistin molecule.
公益社団法人日本薬学会の論文
1970-07-25