Fong W F, Heller J S, Canellakis E S
Biochim Biophys Acta. 1976 Apr 23;428(2):456-65. doi: 10.1016/0304-4165(76)90054-4.
Quiescent, contact inhibited H-35 rat hepatoma cell cultures maintained in minimal essential medium contain a very low level of ornithine decarboxylase activity. However, 2 h after the addition of 10% fetal calf serum to the culture medium, the enzyme activity increases by approx. 100-fold. This increase can be completely inhibited by the simultaneous addition of 10(-2) M putrescine. The presence of putrescine elicits the appearance of an intracellular inhibitor of ornithine decarboxylase. This inhibitor of ornithine decarboxylase has a molecular weight of 26500, is sensitive to the action of chymotrypsin and is noncompetitive with respect to ornithine. The intracellular appearance of this inhibitor is sensitive to cycloheximide but is only partially inhibited by actinomycin D.
在最低限度基本培养基中培养的静止、接触抑制的H-35大鼠肝癌细胞培养物中,鸟氨酸脱羧酶活性水平非常低。然而,向培养基中添加10%胎牛血清2小时后,该酶活性增加约100倍。同时添加10⁻²M腐胺可完全抑制这种增加。腐胺的存在引发了鸟氨酸脱羧酶细胞内抑制剂的出现。这种鸟氨酸脱羧酶抑制剂的分子量为26500,对胰凝乳蛋白酶的作用敏感,对鸟氨酸无竞争性。这种抑制剂在细胞内的出现对放线菌酮敏感,但仅被放线菌素D部分抑制。