Karvonen E, Kauppinen L, Partanen T, Pösö H
Biochem J. 1985 Oct 1;231(1):165-9. doi: 10.1042/bj2310165.
The putrescine-stimulated S-adenosyl-L-methionine decarboxylases from rat liver and yeast were strongly inhibited by Berenil and to a lesser extent by Pentamidine. Ten times greater drug concentrations were needed to achieve a similar level of inhibition of a Mg2+-stimulated bacterial enzyme. The inhibition was irreversible in that extensive dialyses or precipitation with (NH4)2SO4 did not restore enzyme activity. Putrescine did not protect the enzyme against Berenil, but adenosylmethionine either alone or with putrescine partially protected the irreversible action of Berenil. The compound 4,4'-diamidinodiphenylamine, which differs from Berenil only in lacking the azo group between benzene rings, was a weaker inhibitor than Berenil, and its inhibition was reversible. Berenil also inhibited the activity of adenosylmethionine decarboxylase in vivo, by depressing the activity of the enzyme in normal rat liver, for at least 24 h after a single injection (50 mg/kg body wt.) of the drug.
来自大鼠肝脏和酵母的腐胺刺激型S-腺苷-L-蛋氨酸脱羧酶受到贝尼尔的强烈抑制，受到喷他脒的抑制作用较小。对于Mg2+刺激的细菌酶，需要10倍更高的药物浓度才能达到类似的抑制水平。这种抑制是不可逆的，因为广泛透析或用硫酸铵沉淀都不能恢复酶活性。腐胺不能保护该酶免受贝尼尔的抑制，但腺苷甲硫氨酸单独或与腐胺一起能部分保护酶免受贝尼尔的不可逆作用。化合物4,4'-二脒基二苯胺与贝尼尔的区别仅在于苯环之间缺少偶氮基团，它是一种比贝尼尔弱的抑制剂，其抑制作用是可逆的。贝尼尔还能在体内抑制腺苷甲硫氨酸脱羧酶的活性，单次注射（50毫克/千克体重）该药物后，至少24小时内可降低正常大鼠肝脏中该酶的活性。
