Hibasami H, Tanaka M, Nagai J
Chem Biol Interact. 1982 Jul 1;40(3):319-23. doi: 10.1016/0009-2797(82)90154-5.
Activities of aminopropyltransferases (spermidine synthase and spermine synthase) were inhibited by aurintricarboxylic acid (ATA). Spermidine synthase was slightly more sensitive to the inhibitor than spermine synthase. These inhibitions were not prevented by 0.15 M NaCl. Inhibition by ATA of spermidine synthase was 'uncompetitive' with respect to putrescine and that of spermine synthase was 'non-competitive' with respect to spermidine. When the amount of spermidine synthase or spermine synthase was varied, inhibition ratio hardly changed on either case implying no appreciable interaction between ATA and these enzymes.
氨丙基转移酶（亚精胺合酶和精胺合酶）的活性受到金精三羧酸（ATA）的抑制。亚精胺合酶对该抑制剂的敏感性略高于精胺合酶。0.15 M NaCl不能阻止这些抑制作用。ATA对亚精胺合酶的抑制作用相对于腐胺而言是“反竞争性”的，而对精胺合酶的抑制作用相对于亚精胺而言是“非竞争性”的。当亚精胺合酶或精胺合酶的量发生变化时，两种情况下的抑制率几乎没有变化，这意味着ATA与这些酶之间没有明显的相互作用。
