Taguchi Y, Watanabe T, Shiosaka S, Tohyama M, Wada H
Brain Res. 1985 Aug 12;340(2):235-42. doi: 10.1016/0006-8993(85)90919-9.
L-Histidine decarboxylase [L-histidine carboxylyase, HDC, EC 4.1.1.22] is an enzyme distinct from L-DOPA decarboxylase [L-aromatic amino acid carboxylyase, DDC, EC 4.1.1.28]: the two decarboxylases from fetal rat liver were completely separated from each other by DEAE-cellulose column chromatography and by affinity chromatography with L-carnosine as a ligand. The antibody raised against this HDC inhibited the HDC's from rat and guinea-pig brains very strongly, but their DDCs very weakly. However, in immunofluorescent histochemical studies, the antibody cross-reacted with DDC-like immunoreactive structures, such as chromaffin cells of the adrenal medulla, the raphe nucleus, the substantia nigra, and the locus coeruleus of the brain of guinea-pigs, but not of rats, suggesting that these two decarboxylases share some antigenic structures.
L-组氨酸脱羧酶[L-组氨酸羧化酶，HDC，EC 4.1.1.22]是一种与L-多巴脱羧酶[L-芳香族氨基酸羧化酶，DDC，EC 4.1.1.28]不同的酶：通过DEAE-纤维素柱色谱法以及以L-肌肽作为配体的亲和色谱法，可将来自胎鼠肝脏的这两种脱羧酶完全彼此分离。针对这种HDC产生的抗体对大鼠和豚鼠脑内的HDC具有非常强的抑制作用，但对它们的DDC抑制作用非常弱。然而，在免疫荧光组织化学研究中，该抗体与DDC样免疫反应性结构发生交叉反应，如豚鼠脑而非大鼠脑的肾上腺髓质嗜铬细胞、中缝核、黑质和蓝斑，但这表明这两种脱羧酶具有一些共同的抗原结构。
