Ragg H, Kuhn D N, Hahlbrock K
J Biol Chem. 1981 Oct 10;256(19):10061-5.
4-Coumarate:CoA ligase (EC 6.2.1.12) from cell suspension cultures of parsley (Petroselinum hortense) was extensively purified. The enzyme behaved as a monomer with a molecular weight of approximately 60,000. A rabbit antiserum to the purified enzyme was obtained and used to determine the rates of 4-coumarate:CoA ligase synthesis under various conditions of induction, such as short term or continuous irradiation and treatment of the cells with an "elicitor" preparation from a fungal pathogen. In all cases, the time course of changes in the rate of synthesis, measured both in vivo and in vitro, was very similar for 4-coumarate:CoA ligase and a closely related enzyme, phenylalanine ammonia-lyase (EC 4.3.1.5). The results suggest that the mRNA activities encoding the two enzymes are regulated in a coordinated manner.
从欧芹（Petroselinum hortense）细胞悬浮培养物中广泛纯化了4-香豆酸：辅酶A连接酶（EC 6.2.1.12）。该酶表现为单体，分子量约为60,000。获得了针对纯化酶的兔抗血清，并用于测定在各种诱导条件下4-香豆酸：辅酶A连接酶的合成速率，例如短期或连续照射以及用来自真菌病原体的“激发子”制剂处理细胞。在所有情况下，体内和体外测量的4-香豆酸：辅酶A连接酶和密切相关的酶苯丙氨酸解氨酶（EC 4.3.1.5）的合成速率变化的时间进程非常相似。结果表明，编码这两种酶的mRNA活性以协调的方式受到调节。
