Department of Biological Sciences, Union College, Schenectady, New York 12308.
Plant Physiol. 1986 Mar;80(3):798-800. doi: 10.1104/pp.80.3.798.
alpha-dl-Difluoromethylornithine (DFMO), a specific enzyme-activated inhibitor of ornithine decarboxylase, at 0.5 to 2.0 millimolar significantly inhibited mycelial growth and especially sporulation of Helminthosporium maydis in the dark; its inhibitory effect on sporulation was greatly increased under light conditions. Putrescine at 0.25 millimolar fully prevented the inhibitory effects of DFMO; the inhibition caused by the latter could not be prevented by cadaverine or CaCl(2). alpha-dl-Difluoromethylarginine, a specific enzyme-activated inhibitor of arginine decarboxylase, at 0.1 to 2.0 millimolar had a weak inhibitory effect on the fungus. The effect was not dependent on the inhibitor concentration and there was no detectable arginine decarboxylase activity in the fungus.
α-二氟甲基鸟氨酸（DFMO）是一种特异性的酶激活的鸟氨酸脱羧酶抑制剂，在 0.5 至 2.0 毫摩尔浓度下，能显著抑制玉米黑粉病菌丝体的生长，特别是黑暗条件下的孢子形成；在光照条件下，其对孢子形成的抑制作用大大增强。0.25 毫摩尔浓度的腐胺能完全阻止 DFMO 的抑制作用；而后者引起的抑制作用不能被尸胺或 CaCl2 所阻止。α-二氟甲基精氨酸是一种特异性的酶激活的精氨酸脱羧酶抑制剂，在 0.1 至 2.0 毫摩尔浓度下对真菌有较弱的抑制作用。这种作用不依赖于抑制剂浓度，并且真菌中检测不到精氨酸脱羧酶活性。
